Corynebacterium glutamicum genes encoding metabolic pathway proteins

ABSTRACT

Isolated nucleic acid molecules, designated MP nucleic acid molecules, which encode novel MP proteins from  Corynebacterium glutamicum  are described. The invention also provides antisense nucleic acid molecules, recombinant expression vectors containing MP nucleic acid molecules, and host cells into which the expression vectors have been introduced. The invention still further provides isolated MP proteins, mutated MP proteins, fusion proteins, antigenic peptides and methods for the improvement of production of a desired compound from  C. glutamicurn  based on genetic engineering of MP genes in this organism.

RELATED APPLICATIONS

[0001] The present application is an continuation in part of U.S. patent application Ser. No. 09/606,740, filed Jun. 23, 2000. This application is also a continuation in part of U.S. patent application Ser. No. 09/603,124, filed Jun. 23, 2000. The present application claims priority to prior filed U.S. Provisional Patent Application Serial No. 60/141031, filed Jun. 25, 1999, U.S. Provisional Patent Application Serial No. 60/142101, filed Jul. 2, 1999, U.S. Provisional Patent Application Serial No. 60/148613, filed Aug. 12, 1999, U.S. Provisional Patent Application Serial No. 60/187970, filed Mar. 9, 2000, and also to German Patent Application No. 19931420.9, filed Jul. 8, 1999. The entire contents of all of the aforementioned applications are hereby expressly incorporated herein by this reference.

BACKGROUND OF THE INVENTION

[0002] Certain products and by-products of naturally-occurring metabolic processes in cells have utility in a wide array of industries, including the food, feed, cosmetics, and pharmaceutical industries. These molecules, collectively termed ‘fine chemicals’, include organic acids, both proteinogenic and non-proteinogenic amino acids, nucleotides and nucleosides, lipids and fatty acids, diols, carbohydrates, aromatic compounds, vitamins and cofactors, and enzymes. Their production is most conveniently performed through large-scale culture of bacteria developed to produce and secrete large quantities of a particular desired molecule. One particularly useful organism for this purpose is Corynebacterium glutamicum, a gram positive, nonpathogenic bacterium. Through strain selection, a number of mutant strains have been developed which produce an array of desirable compounds. However, selection of strains improved for the production of a particular molecule is a time-consuming and difficult process.

SUMMARY OF THE INVENTION

[0003] The invention provides novel bacterial nucleic acid molecules which have a variety of uses. These uses include the identification of microorganisms which can be used to produce fine chemicals (e.g., amino acids, such as, for example, lysine and methionine), the modulation of fine chemical production in C. glutamicum or related bacteria, the typing or identification of C. glutamicum or related bacteria, as reference points for mapping the C. glutamicum genome, and as markers for transformation. These novel nucleic acid molecules encode proteins, referred to herein as metabolic pathway (MP) proteins.

[0004]C. glutamicum is a gram positive, aerobic bacterium which is commonly used in industry for the large-scale production of a variety of fine chemicals, and also for the degradation of hydrocarbons (such as in petroleum spills) and for the oxidation of terpenoids. The MP nucleic acid molecules of the invention, therefore, can be used to identify microorganisms which can be used to produce fine chemicals, e.g., by fermentation processes. Modulation of the expression of the MP nucleic acids of the invention, or modification of the sequence of the MP nucleic acid molecules of the invention, can be used to modulate the production of one or more fine chemicals from a microorganism (e.g., to improve the yield or production of one or more fine chemicals from a Corynebacterium or Brevibacterium species). In a preferred embodiment, the MP genes of the invention are combined with one or more genes involved in the same or different metabolic pathway to modulate the production of one or more fine chemicals from a microorganism.

[0005] The MP nucleic acids of the invention may also be used to identify an organism as being Corynebacterium glutamicum or a close relative thereof, or to identify the presence of C. glutamicum or a relative thereof in a mixed population of microorganisms. The invention provides the nucleic acid sequences of a number of C. glutamicum genes; by probing the extracted genomic DNA of a culture of a unique or mixed population of microorganisms under stringent conditions with a probe spanning a region of a C. glutamicum gene which is unique to this organism, one can ascertain whether this organism is present. Although Corynebacterium glutamicum itself is nonpathogenic, it is related to species pathogenic in humans, such as Corynebacterium diphtheriae (the causative agent of diphtheria); the detection of such organisms is of significant clinical relevance.

[0006] The MP nucleic acid molecules of the invention may also serve as reference points for mapping of the C. glutamicum genome, or of genomes of related organisms. Similarly, these molecules, or variants or portions thereof, may serve as markers for genetically engineered Corynebacterium or Brevibacterium species.

[0007] The MP proteins encoded by the novel nucleic acid molecules of the invention are capable of, for example, performing an enzymatic step involved in the metabolism of certain fine chemicals, including amino acids, e.g., lysine and methionine, vitamins, cofactors, nutraceuticals, nucleotides, nucleosides, and trehalose. Given the availability of cloning vectors for use in Corynebacterium glutamicum, such as those disclosed in Sinskey et al., U.S. Pat. No. 4,649,119, and techniques for genetic manipulation of C. glutamicum and the related Brevibacterium species (e.g., lactofermentum) (Yoshihama et al, J. Bacteriol. 162: 591-597 (1985); Katsumata et al., J. Bacteriol. 159: 306-311 (1984); and Santamaria et al., J. Gen. Microbiol. 130: 2237-2246 (1984)), the nucleic acid molecules of the invention may be utilized in the genetic engineering of this organism to make it a better or more efficient producer of one or more fine chemicals.

[0008] This improved production or efficiency of production of a fine chemical may be due to a direct effect of manipulation of a gene of the invention, or it may be due to an indirect effect of such manipulation. Specifically, alterations in C. glutamicum metabolic pathways for amino acids, e.g, lysine and methionine, vitamins, cofactors, nucleotides, and trehalose may have a direct impact on the overall production of one or more of these desired compounds from this organism. For example, optimizing the activity of a lysine or a methionine biosynthetic pathway protein or decreasing the activity of a lysine or methionine degradative pathway protein may result in an increase in the yield or efficiency of production of lysine or methionine from such an engineered organism. Alterations in the proteins involved in these metabolic pathways may also have an indirect impact on the production or efficiency of production of a desired fine chemical. For example, a reaction which is in competition for an intermediate necessary for the production of a desired molecule may be eliminated, or a pathway necessary for the production of a particular intermediate for a desired compound may be optimized. Further, modulations in the biosynthesis or degradation of, for example, an amino acid, e.g., lysine or methionine, a vitamin, or a nucleotide may increase the overall ability of the microorganism to rapidly grow and divide, thus increasing the number and/or production capacities of the microorganism in culture and thereby increasing the possible yield of the desired fine chemical.

[0009] The nucleic acid and protein molecules of the invention, alone or in combination with one or more nucleic acid and protein molecules of the same or different metabolic pathway, may be utilized to directly improve the production or efficiency of production of one or more desired fine chemicals from Corynebacterium glutamicum (e.g., methionine or lysine). Using recombinant genetic techniques well known in the art, one or more of the biosynthetic or degradative enzymes of the invention for amino acids, e.g., lysine and methionine, vitamins, cofactors, nutraceuticals, nucleotides, nucleosides, or trehalose may be manipulated such that its function is modulated. For example, a biosynthetic enzyme may be improved in efficiency, or its allosteric control region destroyed such that feedback inhibition of production of the compound is prevented. Similarly, a degradative enzyme may be deleted or modified by substitution, deletion, or addition such that its degradative activity is lessened for the desired compound without impairing the viability of the cell. In each case, the overall yield or rate of production of the desired fine chemical may be increased.

[0010] It is also possible that such alterations in the protein and nucleotide molecules of the invention may improve the production of other fine chemicals besides the amino acids, e.g., lysine and methionine, vitamins, cofactors, nutraceuticals, nucleotides, nucleosides, and trehalose through indirect mechanisms. Metabolism of any one compound is necessarily intertwined with other biosynthetic and degradative pathways within the cell, and necessary cofactors, intermediates, or substrates in one pathway are likely supplied or limited by another such pathway. Therefore, by modulating the activity of one or more of the proteins of the invention, the production or efficiency of activity of another fine chemical biosynthetic or degradative pathway may be impacted. For example, amino acids serve as the structural units of all proteins, yet may be present intracellularly in levels which are limiting for protein synthesis; therefore, by increasing the efficiency of production or the yields of one or more amino acids within the cell, proteins, such as biosynthetic or degradative proteins, may be more readily synthesized. Likewise, an alteration in a metabolic pathway enzyme such that a particular side reaction becomes more or less favored may result in the over- or under-production of one or more compounds which are utilized as intermediates or substrates for the production of a desired fine chemical.

[0011] This invention provides novel nucleic acid molecules which encode proteins, referred to herein as metabolic pathway (“MP”) proteins, which are capable of, for example, performing an enzymatic step involved in the metabolism of molecules important for the normal functioning of cells, such as amino acids, e.g., lysine and methionine, vitamins, cofactors, nucleotides and nucleosides, or trehalose. Nucleic acid molecules encoding an MP protein are referred to herein as MP nucleic acid molecules. In a preferred embodiment, an MP protein, alone or in combination with one or more proteins of the same or different metabolic pathway, performs an enzymatic step related to the metabolism of one or more of the following: amino acids, e.g., lysine and methionine, vitamins, cofactors, nutraceuticals, nucleotides, nucleosides, and trehalose. Examples of such proteins include those encoded by the genes set forth in Table 1.

[0012] Accordingly, one aspect of the invention pertains to isolated nucleic acid molecules (e.g., cDNAs, DNAs, or RNAs) comprising a nucleotide sequence encoding an MP protein or biologically active portions thereof, as well as nucleic acid fragments suitable as primers or hybridization probes for the detection or amplification of MP-encoding nucleic acid (e.g., DNA or mRNA). In particularly preferred embodiments, the isolated nucleic acid molecule comprises one of the nucleotide sequences set forth as the odd-numbered SEQ ID NO in the Sequence Listing (e.g., SEQ ID NO: 1, SEQ ID NO:3, or SEQ ID NO:5), or the coding region or a complement thereof of one of these nucleotide sequences. In other particularly preferred embodiments, the isolated nucleic acid molecule of the invention comprises a nucleotide sequence which hybridizes to or is at least about 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, or 60%, preferably at least about 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, or 70%%, more preferably at least about 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, or 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, or 90%, or 91%, 92%, 93%, 94%, and even more preferably at least about 95%, 96%, 97%, 98%, 99%, 99.7% or more homologous to a nucleotide sequence set forth as an odd-numbered SEQ ID NO in the Sequence Listing (e.g., SEQ ID NO: 1, SEQ ID NO:3, or SEQ ID NO:5), or a portion thereof. In other preferred embodiments, the isolated nucleic acid molecule encodes one of the amino acid sequences set forth as an even-numbered SEQ ID NO in the Sequence Listing (e.g., SEQ ID NO:2, SEQ ID NO:4, or SEQ ID NO:6). The preferred MP proteins of the present invention also preferably possess at least one of the MP activities described herein.

[0013] In another embodiment, the isolated nucleic acid molecule encodes a protein or portion thereof wherein the protein or portion thereof includes an amino acid sequence which is sufficiently homologous to an amino acid sequence of the invention (e.g., a sequence having an even-numbered SEQ ID NO in the Sequence Listing, such as SEQ ID NO:2, SEQ ID NO:4, or SEQ ID NO:6), e.g., sufficiently homologous to an amino acid sequence of the invention such that the protein or portion thereof maintains an MP activity. Preferably, the protein or portion thereof encoded by the nucleic acid molecule maintains the ability to perform an enzymatic reaction in a amino acid, e.g., lysine or methionine, vitamin, cofactor, nutraceutical, nucleotide, nucleoside, or trehalose metabolic pathway. In one embodiment, the protein encoded by the nucleic acid molecule is at least about 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, or 60%, preferably at least about 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, or 70%%, more preferably at least about 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, or 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, or 90%, or 91%, 92%, 93%, 94%, and even more preferably at least about 95%, 96%, 97%, 98%, 99%, 99.7% or more homologous to an amino acid sequence of the invention (e.g., an entire amino acid sequence selected from those having an even-numbered SEQ ID NO in the Sequence Listing, such as SEQ ID NO:2, SEQ ID NO:4, or SEQ ID NO:6). In another preferred embodiment, the protein is a full length C. glutamicum protein which is substantially homologous to an entire amino acid sequence of the invention (encoded by an open reading frame shown in the corresponding odd-numbered SEQ ID NO in the Sequence Listing (e.g., SEQ ID NO:1, SEQ ID NO:3, or SEQ ID NO:5).

[0014] In another preferred embodiment, the isolated nucleic acid molecule is derived from C. glutamicum and encodes a protein (e.g., an MP fusion protein) which includes a biologically active domain which is at least about 50% or more homologous to one of the amino acid sequences of the invention (e.g., a sequence of one of the even-numbered SEQ ID NOs in the Sequence Listing, such as SEQ ID NO:2, SEQ ID NO:4, or SEQ ID NO:6) and is able to catalyze a reaction in a metabolic pathway for an amino acid, e.g., lysine or methionine, vitamin, cofactor, nutraceutical, nucleotide, nucleoside, or trehalose, or one or more of the activities set forth in Table 1, and which also includes heterologous nucleic acid sequences encoding a heterologous polypeptide or regulatory regions.

[0015] In another embodiment, the isolated nucleic acid molecule is at least 15 nucleotides in length and hybridizes under stringent conditions to a nucleic acid molecule comprising a nucleotide sequence of the invention (e.g., a sequence of an odd-numbered SEQ ID NO in the Sequence Listing, such as SEQ ID NO: 1, SEQ ID NO:3, or SEQ ID NO:5). Preferably, the isolated nucleic acid molecule corresponds to a naturally-occurring nucleic acid molecule. More preferably, the isolated nucleic acid encodes a naturally-occurring C. glutamicum MP protein, or a biologically active portion thereof.

[0016] Another aspect of the invention pertains to vectors, e.g., recombinant expression vectors, containing the nucleic acid molecules of the invention, alone or in combination with one or more nucleic acid molecules involved in the same or different pathway, and host cells into which such vectors have been introduced. In one embodiment, such a host cell is used to produce an MP protein by culturing the host cell in a suitable medium. The MP protein can be then isolated from the medium or the host cell.

[0017] Yet another aspect of the invention pertains to a genetically altered microorganism in which one or more MP genes, alone or in combination with one or more genes involved in the same or different metabolic pathway, have been introduced or altered. In one embodiment, the genome of the microorganism has been altered by introduction of a nucleic acid molecule of the invention encoding one or more wild-type or mutated MP sequences as transgenes alone or in combination with one or more nucleic acid molecules involved in the same or different metabolic pathway. In another embodiment, one or more endogenous MP genes within the genome of the microorganism have been altered, e.g., functionally disrupted, by homologous recombination with one or more altered MP genes. In another embodiment, one or more endogenous or introduced MP genes, alone or in combination with one or more genes of the same or different metabolic pathway in a microorganism have been altered by one or more point mutations, deletions, or inversions, but still encode functional MP proteins. In still another embodiment, one or more of the regulatory regions (e.g., a promoter, repressor, or inducer) of one or more MP genes in a microorganism, alone or in combination with one or more MP genes or in combination with one or more genes of the same or different metabolic pathway, has been altered (e.g., by deletion, truncation, inversion, or point mutation) such that the expression of one or more MP genes is modulated. In a preferred embodiment, the microorganism belongs to the genus Corynebacterium or Brevibacterium, with Corynebacterium glutamicum being particularly preferred. In a preferred embodiment, the microorganism is also utilized for the production of a desired compound, such as an amino acid, with lysine and methionine being particularly preferred. In a particularly preferred embodiment, the MP gene is the metZ gene (SEQ ID NO:1), metC gene (SEQ ID NO:3), or the RXA00657 gene (SEQ ID NO:5), alone or in combination with one or more MP genes of the invention or in combination with one or more genes involved in methionine and/or lysine metabolism.

[0018] In another aspect, the invention provides a method of identifying the presence or activity of Cornyebacterium diphtheriae in a subject. This method includes detection of one or more of the nucleic acid or amino acid sequences of the invention (e.g., the sequences set forth in Table 1 and in the Sequence Listing as SEQ ID NOs 1 through 122) in a subject, thereby detecting the presence or activity of Corynebacterium diphtheriae in the subject.

[0019] Still another aspect of the invention pertains to an isolated MP protein or portion, e.g., biologically active portion, thereof. In a preferred embodiment, the isolated MP protein or portion thereof, alone or in combination with one or more MP proteins of the invention or in combination with one or more proteins of the same or different metabolic pathway, can catalyze an enzymatic reaction involved in one or more pathways for the metabolism of an amino acid, e.g., lysine or methionine, a vitamin, a cofactor, a nutraceutical, a nucleotide, a nucleoside, or trehalose. In another preferred embodiment, the isolated MP protein or portion thereof, is sufficiently homologous to an amino acid sequence of the invention (e.g., a sequence of an even-numbered SEQ ID NO: in the Sequence Listing, such as SEQ ID NO:2, SEQ ID NO:4, or SEQ ID NO:6) such that the protein or portion thereof maintains the ability to catalyze an enzymatic reaction involved in one or more pathways for the metabolism of an amino acid, a vitamin, a cofactor, a nutraceutical, a nucleotide, a nucleoside, or trehalose.

[0020] The invention also provides an isolated preparation of an MP protein. In preferred embodiments, the MP protein comprises an amino acid sequence of the invention (e.g., a sequence of an even-numbered SEQ ID NO: of the Sequence Listing such as SEQ ID NO:2, SEQ ID NO:4, or SEQ ID NO:6). In another preferred embodiment, the invention pertains to an isolated full length protein which is substantially homologous to an entire amino acid sequence of the invention (e.g., a sequence of an even-numbered SEQ ID NO of the Sequence Listing such as SEQ ID NO:2, SEQ ID NO:4, or SEQ ID NO:6) (encoded by an open reading frame set forth in a corresponding odd-numbered SEQ ID NO: of the Sequence Listing such as SEQ ID NO:1, SEQ ID NO:3, or SEQ ID NO:5). In yet another embodiment, the protein is at least about 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, or 60%, preferably at least about 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, or 70%%, more preferably at least about 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, or 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, or 90%, or 91%, 92%, 93%, 94%, and even more preferably at least about 95%, 96%, 97%, 98%, 99%, 99.7% or more homologous to an entire amino acid sequence of the invention (e.g., a sequence of an even-numbered SEQ ID NO: of the Sequence Listing such as SEQ ID NO:2, SEQ ID NO:4, or SEQ ID NO:6). In other embodiments, the isolated MP protein comprises an amino acid sequence which is at least about 50% or more homologous to one of the amino acid sequences of the invention (e.g., a sequence of an even-numbered SEQ ID NO: of the Sequence Listing such as SEQ ID NO:2, SEQ ID NO:4, or SEQ ID NO:6) and is able to catalyze an enzymatic reaction in an amino acid, vitamin, cofactor, nutraceutical, nucleotide, nucleoside, or trehalose metabolic pathway either alone or in combination one or more MP proteins of the invention or any protein of the same or different metabolic pathway, or has one or more of the activities set forth in Table 1.

[0021] Alternatively, the isolated MP protein can comprise an amino acid sequence which is encoded by a nucleotide sequence which hybridizes, e.g., hybridizes under stringent conditions, or is at least about 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, or 60%, preferably at least about 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, or 70%%, more preferably at least about 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, or 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, or 90%, or 91%, 92%, 93%, 94%, and even more preferably at least about 95%, 96%, 97%, 98%, 99%, 99.7% or more homologous to a nucleotide sequence of one of the even-numbered SEQ ID NOs set forth in the Sequence Listing. It is also preferred that the preferred forms of MP proteins also have one or more of the MP bioactivities described herein.

[0022] The MP polypeptide, or a biologically active portion thereof, can be operatively linked to a non-MP polypeptide to form a fusion protein. In preferred embodiments, this fusion protein has an activity which differs from that of the MP protein alone. In other preferred embodiments, this fusion protein, when introduced into a C. glutamicum pathway for the metabolism of an amino acid, vitamin, cofactor, nutraceutical, results in increased yields and/or efficiency of production of a desired fine chemical from C. glutamicum. In particularly preferred embodiments, integration of this fusion protein into an amino acid, vitamin, cofactor, nutraceutical, nucleotide, nucleoside, or trehalose metabolic pathway of a host cell modulates production of a desired compound from the cell.

[0023] In another aspect, the invention provides methods for screening molecules which modulate the activity of an MP protein, either by interacting with the protein itself or a substrate or binding partner of the MP protein, or by modulating the transcription or translation of an MP nucleic acid molecule of the invention.

[0024] Another aspect of the invention pertains to a method for producing a fine chemical. This method involves the culturing of a cell containing one or more vectors directing the expression of one or more MP nucleic acid molecules of the either alone or in combination one or more MP nucleic acid molecules of the invention or any nucleic acid molecule of the same or different metabolic pathway, such that a fine chemical is produced. In a preferred embodiment, this method further includes the step of obtaining a cell containing such a vector, in which a cell is transfected with a vector directing the expression of an MP nucleic acid. In another preferred embodiment, this method further includes the step of recovering the fine chemical from the culture. In a particularly preferred embodiment, the cell is from the genus Corynebacterium or Brevibacterium, or is selected from those strains set forth in Table 3. In another preferred embodiment, the MP genes is the metZ gene (SEQ ID NO: 1), metC gene (SEQ ID NO:3), or the gene designated as RXA00657 (SEQ ID NO:5) (see Table 1), alone or in combination with one or more MP nucleic acid molecules of the invention or with one or more genes involved in methionine and/or lysine metabolism. In yet another preferred embodiment, the fine chemical is an amino acid, e.g., L-lysine and L-methionine.

[0025] Another aspect of the invention pertains to methods for modulating production of a molecule from a microorganism. Such methods include contacting the cell with an agent which modulates MP protein activity or MP nucleic acid expression such that a cell associated activity is altered relative to this same activity in the absence of the agent. In a preferred embodiment, the cell is modulated for one or more C. glutamicum amino acid, vitamin, cofactor, nutraceutical, nucleotide, nucleoside, or trehalose metabolic pathways, such that the yields or rate of production of a desired fine chemical by this microorganism is improved. The agent which modulates MP protein activity can be an agent which stimulates MP protein activity or MP nucleic acid expression. Examples of agents which stimulate MP protein activity or MP nucleic acid expression include small molecules, active MP proteins, and nucleic acids encoding MP proteins that have been introduced into the cell. Examples of agents which inhibit MP activity or expression include small molecules and antisense MP nucleic acid molecules.

[0026] Another aspect of the invention pertains to methods for modulating yields of a desired compound from a cell, involving the introduction of a wild-type or mutant MP gene into a cell, either alone or in combination one or more MP nucleic acid molecules of the invention or any nucleic acid molecule of the same or different metabolic pathway, either maintained on a separate plasmid or integrated into the genome of the host cell. If integrated into the genome, such integration can be random, or it can take place by homologous recombination such that the native gene is replaced by the introduced copy, causing the production of the desired compound from the cell to be modulated. In a preferred embodiment, said yields are increased. In another preferred embodiment, said chemical is a fine chemical. In a particularly preferred embodiment, said fine chemical is an amino acid. In especially preferred embodiments, said amino acid are L-lysine and L-methionine. In another preferred embodiment, said gene is the metZ gene (SEQ ID NO:1), metC gene (SEQ ID NO:3), or the RXA00657 gene (SEQ ID NO:5), alone or in combination with one or more MP nucleic acid molecules of the invention or with one or more genes involved in methionine and/or lysine metabolism.

DETAILED DESCRIPTION OF THE INVENTION

[0027] The present invention provides MP nucleic acid and protein molecules which are involved in the metabolism of certain fine chemicals in Corynebacterium glutamicum, including amino acids, e.g., lysine and methionine, vitamins, cofactors, nutraceuticals, nucleotides, nucleosides, and trehalose. The molecules of the invention may be utilized in the modulation of production of fine chemicals from microorganisms, such as C. glutamicum, either directly (e.g., where modulation of the activity of a lysine or methionine biosynthesis protein has a direct impact on the production or efficiency of production of lysine or methionine from that organism), or may have an indirect impact which nonetheless results in an increase of yield or efficiency of production of the desired compound (e.g., where modulation of the activity of a nucleotide biosynthesis protein has an impact on the production of an organic acid or a fatty acid from the bacterium, perhaps due to improved growth or an increased supply of necessary cofactors, energy compounds, or precursor molecules). The MP molecules may be utilized alone or in combination with other MP molecules of the invention, or in combination with other molecules involved in the same or a different metabolic pathway (e.g., lysine or methione metabolism). In a preferred embodiment, the MP molecules are the metZ (SEQ ID NO: 1), metC (SEQ ID NO:3), or RXA00657 (SEQ ID NO:5) nucleic acid molecules and the proteins encoded by these nucleic acid molecules (SEQ ID NO:2, SEQ ID NO.:4 and SEQ ID NO.:6, respectively). Aspects of the invention are further explicated below.

[0028] I. Fine Chemicals

[0029] The term ‘fine chemical’ is art-recognized and includes molecules produced by an organism which have applications in various industries, such as, but not limited to, the pharmaceutical, agriculture, and cosmetics industries. Such compounds include organic acids, such as tartaric acid, itaconic acid, and diaminopimelic acid, both proteinogenic and non-proteinogenic amino acids, purine and pyrimidine bases, nucleosides, and nucleotides (as described e.g. in Kuninaka, A. (1996) Nucleotides and related compounds, p. 561-612, in Biotechnology vol. 6, Rehm et al., eds. VCH: Weinheim, and references contained therein), lipids, both saturated and unsaturated fatty acids (e.g., arachidonic acid), diols (e.g., propane diol, and butane diol), carbohydrates (e.g., hyaluronic acid and trehalose), aromatic compounds (e.g., aromatic amines, vanillin, and indigo), vitamins and cofactors (as described in Ullmann's Encyclopedia of Industrial Chemistry, vol. A27, “Vitamins”, p. 443-613 (1996) VCH: Weinheim and references therein; and Ong, A. S., Niki, E. & Packer, L. (1995) “Nutrition, Lipids, Health, and Disease” Proceedings of the UNESCO/Confederation of Scientific and Technological Associations in Malaysia, and the Society for Free Radical Research—Asia, held Sep. 1-3, 1994 at Penang, Malaysia, AOCS Press, (1995)), enzymes, polyketides (Cane et al. (1998) Science 282: 63-68), and all other chemicals described in Gutcho (1983) Chemicals by Fermentation, Noyes Data Corporation, ISBN: 0818805086 and references therein. The metabolism and uses of certain of these fine chemicals are further explicated below.

[0030] A. Amino Acid Metabolism and Uses

[0031] Amino acids comprise the basic structural units of all proteins, and as such are essential for normal cellular functioning in all organisms. The term “amino acid” is art-recognized. The proteinogenic amino acids, of which there are 20 species, serve as structural units for proteins, in which they are linked by peptide bonds, while the nonproteinogenic amino acids (hundreds of which are known) are not normally found in proteins (see Ulmann's Encyclopedia of Industrial Chemistry, vol. A2, p. 57-97 VCH: Weinheim (1985)). Amino acids may be in the D- or L- optical configuration, though L-amino acids are generally the only type found in naturally-occurring proteins. Biosynthetic and degradative pathways of each of the 20 proteinogenic amino acids have been well characterized in both prokaryotic and eukaryotic cells (see, for example, Stryer, L. Biochemistry, 3^(rd) edition, pages 578-590 (1988)). The ‘essential’ amino acids (histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine), so named because they are generally a nutritional requirement due to the complexity of their biosyntheses, are readily converted by simple biosynthetic pathways to the remaining 11 ‘nonessential’ amino acids (alanine, arginine, asparagine, aspartate, cysteine, glutamate, glutamine, glycine, proline, serine, and tyrosine). Higher animals do retain the ability to synthesize some of these amino acids, but the essential amino acids must be supplied from the diet in order for normal protein synthesis to occur.

[0032] Aside from their function in protein biosynthesis, these amino acids are interesting chemicals in their own right, and many have been found to have various applications in the food, feed, chemical, cosmetics, agriculture, and pharmaceutical industries. Lysine is an important amino acid in the nutrition not only of humans, but also of monogastric animals such as poultry and swine. Glutamate is most commonly used as a flavor additive (mono-sodium glutamate, MSG) and is widely used throughout the food industry, as are aspartate, phenylalanine, glycine, and cysteine. Glycine, L-methionine and tryptophan are all utilized in the pharmaceutical industry. Glutamine, valine, leucine, isoleucine, histidine, arginine, proline, serine and alanine are of use in both the pharmaceutical and cosmetics industries. Threonine, tryptophan, and D/L-methionine are common feed additives. (Leuchtenberger, W. (1996) Amino aids—technical production and use, p. 466-502 in Rehm et al. (eds.) Biotechnology vol. 6, chapter 14a, VCH: Weinheim). Additionally, these amino acids have been found to be useful as precursors for the synthesis of synthetic amino acids and proteins, such as N-acetylcysteine, S-carboxymethyl-L-cysteine, (S)-5-hydroxytryptophan, and others described in Ulmann's Encyclopedia of Industrial Chemistry, vol. A2, p. 57-97, VCH: Weinheim, 1985.

[0033] The biosynthesis of these natural amino acids in organisms cabable of producing them, such as bacteria, has been well characterized (for review of bacterial amino acid biosynthesis and regulation thereof, see Umbarger, H. E. (1978) Ann. Rev. Biochem. 47: 533-606). Glutamate is synthesized by the reductive amination of α-ketoglutarate, an intermediate in the citric acid cycle. Glutamine, proline, and arginine are each subsequently produced from glutamate. The biosynthesis of serine is a three-step process beginning with 3-phosphoglycerate (an intermediate in glycolysis), and resulting in this amino acid after oxidation, transamination, and hydrolysis steps. Both cysteine and glycine are produced from serine; the former by the condensation of homocysteine with serine, and the latter by the transferal of the side-chain β-carbon atom to tetrahydrofolate, in a reaction catalyzed by serine transhydroxymethylase. Phenylalanine and tyrosine are synthesized from the glycolytic and pentose phosphate pathway precursors erythrose 4-phosphate and phosphoenolpyruvate in a 9-step biosynthetic pathway that differ only at the final two steps after synthesis of prephenate. Tryptophan is also produced from these two initial molecules, but its synthesis is an 11-step pathway. Tyrosine may also be synthesized from phenylalanine, in a reaction catalyzed by phenylalanine hydroxylase. Alanine, valine, and leucine are all biosynthetic products of pyruvate, the final product of glycolysis. Aspartate is formed from oxaloacetate, an intermediate of the citric acid cycle. Asparagine, methionine, threonine, and lysine are each produced by the conversion of aspartate. Isoleucine is formed from threonine.

[0034] The biosynthetic pathways leading to methionine have been studied in diverse organisms. The first step, acylation of homoserine, is common to all of the organisms, even though the source of the transferred acyl groups is different. Escherichia coli and the related species use succinyl-CoA (Michaeli, S. and Ron, E. Z. (1981) Mol. Gen. Genet. 182, 349-354), while Saccharomyces cerevisiae (Langin, T., et al. (1986) Gene 49, 283-293), Brevibacterium flavum (Miyajima, R. and Shiio, I. (1973) J. Biochem. 73, 1061-1068; Ozaki, H. and Shiio, I. (1982) J. Biochem. 91, 1163-1171), C. glutamicum (Park, S.-D., et al. (1998) Mol. Cells 8, 286-294), and Leptospira meyeri (Belfaiza, J. et al. (1998) 180, 250-255; Bourhy, P., et al. (1997) J. Bacteriol. 179, 4396-4398) use acetyl-CoA as the acyl donor. Formation of homocysteine from acylhomoserine can occur in two different ways. E. coli uses the transsulfuration pathway which is catalyzed by cystathionine γ-synthase (the product of metB) and cystathionine β-lyase (the product of metC). S. cerevisiae (Cherest, H. and Surdin-Kerjan, Y. (1992) Genetics 130, 51-58), B. flavum (Ozaki, H. and Shiio, I. (1982) J. Biochem. 91, 1163-1171), Pseudomonas aeruginosa (Foglino, M., et al. (1995) Microbiology 141, 431-439), and L. meyeri (Belfaiza, J., et al. (1998) J. Bacteriol. 180, 250-255) utilize the direct sulfhydrylation pathway which is catalyzed by acylhomoserine sulfhydrylase. Unlike closely related B. flavum which uses only the direct sulfhydrylation pathway, enzyme activities of the transsulfuration pathway have been detected in the extracts of the C. glutamicum cells and the pathway has been proposed to be the route for methionine biosynthesis in the organism (Hwang, B-J., et al. (1999) Mol. Cells 9, 300-308; Kase, H. and Nakayama, K. (1974) Agr. Biol. Chem. 38, 2021-2030; Park, S.-D., et al. 1998) Mol. Cells 8, 286-294).

[0035] Although some genes involved in methionine biosynthesis in C. glutamicum have been isolated, information on the biosynthesis of methionine in C. glutamicum is still very limited. No genes other than metA and metB have been isolated from the organism. To understand the biosynthetic pathways leading to methionine in C. glutamicum, we have isolated and characterized the metC gene (SEQ ID NO:3) and the metZ (also called metY) gene (SEQ ID NO: 1) of C. glutamicum (see Table 1).

[0036] Amino acids in excess of the protein synthesis needs of the cell cannot be stored, and are instead degraded to provide intermediates for the major metabolic pathways of the cell (for review see Stryer, L. Biochemistry 3^(rd) ed. Ch. 21 “Amino Acid Degradation and the Urea Cycle” p. 495-516 (1988)). Although the cell is able to convert unwanted amino acids into useful metabolic intermediates, amino acid production is costly in terms of energy, precursor molecules, and the enzymes necessary to synthesize them. Thus it is not surprising that amino acid biosynthesis is regulated by feedback inhibition, in which the presence of a particular amino acid serves to slow or entirely stop its own production (for overview of feedback mechanisms in amino acid biosynthetic pathways, see Stryer, L. Biochemistry, 3^(rd) ed. Ch. 24: “Biosynthesis of Amino Acids and Heme” p. 575-600 (1988)). Thus, the output of any particular amino acid is limited by the amount of that amino acid present in the cell.

[0037] B. Vitamin, Cofactor, and Nutraceutical Metabolism and Uses

[0038] Vitamins, cofactors, and nutraceuticals comprise another group of molecules which the higher animals have lost the ability to synthesize and so must ingest, although they are readily synthesized by other organisms, such as bacteria. These molecules are either bioactive substances themselves, or are precursors of biologically active substances which may serve as electron carriers or intermediates in a variety of metabolic pathways. Aside from their nutritive value, these compounds also have significant industrial value as coloring agents, antioxidants, and catalysts or other processing aids. (For an overview of the structure, activity, and industrial applications of these compounds, see, for example, Ullman's Encyclopedia of Industrial Chemistry, “Vitamins” vol. A27, p. 443-613, VCH: Weinheim, 1996.) The term “vitamin” is art-recognized, and includes nutrients which are required by an organism for normal functioning, but which that organism cannot synthesize by itself. The group of vitamins may encompass cofactors and nutraceutical compounds. The language “cofactor” includes nonproteinaceous compounds required for a normal enzymatic activity to occur. Such compounds may be organic or inorganic; the cofactor molecules of the invention are preferably organic. The term “nutraceutical” includes dietary supplements having health benefits in plants and animals, particularly humans. Examples of such molecules are vitamins, antioxidants, and also certain lipids (e.g., polyunsaturated fatty acids).

[0039] The biosynthesis of these molecules in organisms capable of producing them, such as bacteria, has been largely characterized (Ullman's Encyclopedia of Industrial Chemistry, “Vitamins” vol. A27, p. 443-613, VCH: Weinheim, 1996; Michal, G. (1999) Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology, John Wiley & Sons; Ong, A. S., Niki, E. & Packer, L. (1995) “Nutrition, Lipids, Health, and Disease” Proceedings of the UNESCO/Confederation of Scientific and Technological Associations in Malaysia, and the Society for Free Radical Research—Asia, held Sep. 1-3, 1994 at Penang, Malaysia, AOCS Press: Champaign, Ill. X, 374 S).

[0040] Thiamin (vitamin B₁) is produced by the chemical coupling of pyrimidine and thiazole moieties. Riboflavin (vitamin B₂) is synthesized from guanosine-5′-triphosphate (GTP) and ribose-5′-phosphate. Riboflavin, in turn, is utilized for the synthesis of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD). The family of compounds collectively termed ‘vitamin B₆’ (e.g., pyridoxine, pyridoxamine, pyridoxa-5′-phosphate, and the commercially used pyridoxin hydrochloride) are all derivatives of the common structural unit, 5-hydroxy-6-methylpyridine. Pantothenate (pantothenic acid, (R)-(+)-N-(2,4-dihydroxy-3,3-dimethyl-1-oxobutyl)-β-alanine) can be produced either by chemical synthesis or by fermentation. The final steps in pantothenate biosynthesis consist of the ATP-driven condensation of β-alanine and pantoic acid. The enzymes responsible for the biosynthesis steps for the conversion to pantoic acid, to β-alanine and for the condensation to panthotenic acid are known. The metabolically active form of pantothenate is Coenzyme A, for which the biosynthesis proceeds in 5 enzymatic steps. Pantothenate, pyridoxal-5′-phosphate, cysteine and ATP are the precursors of Coenzyme A. These enzymes not only catalyze the formation of panthothante, but also the production of (R)-pantoic acid, (R)-pantolacton, (R)-panthenol (provitamin B₅), pantetheine (and its derivatives) and coenzyme A.

[0041] Biotin biosynthesis from the precursor molecule pimeloyl-CoA in microorganisms has been studied in detail and several of the genes involved have been identified. Many of the corresponding proteins have been found to also be involved in Fe-cluster synthesis and are members of the nifS class of proteins. Lipoic acid is derived from octanoic acid, and serves as a coenzyme in energy metabolism, where it becomes part of the pyruvate dehydrogenase complex and the α-ketoglutarate dehydrogenase complex. The folates are a group of substances which are all derivatives of folic acid, which is turn is derived from L-glutamic acid, p-amino-benzoic acid and 6-methylpterin. The biosynthesis of folic acid and its derivatives, starting from the metabolism intermediates guanosine-5′-triphosphate (GTP), L-glutamic acid and p-amino-benzoic acid has been studied in detail in certain microorganisms.

[0042] Corrinoids (such as the cobalamines and particularly vitamin B₁₂) and porphyrines belong to a group of chemicals characterized by a tetrapyrole ring system. The biosynthesis of vitamin B₁₂ is sufficiently complex that it has not yet been completely characterized, but many of the enzymes and substrates involved are now known. Nicotinic acid (nicotinate), and nicotinamide are pyridine derivatives which are also termed ‘niacin’. Niacin is the precursor of the important coenzymes NAD (nicotinamide adenine dinucleotide) and NADP (nicotinamide adenine dinucleotide phosphate) and their reduced forms.

[0043] The large-scale production of these compounds has largely relied on cell-free chemical syntheses, though some of these chemicals have also been produced by large-scale culture of microorganisms, such as riboflavin, Vitamin B₆, pantothenate, and biotin. Only Vitamin B₁₂ is produced solely by fermentation, due to the complexity of its synthesis. In vitro methodologies require significant inputs of materials and time, often at great cost.

[0044] C. Purine, Pyrimidine, Nucleoside and Nucleotide Metabolism and Uses

[0045] Purine and pyrimidine metabolism genes and their corresponding proteins are important targets for the therapy of tumor diseases and viral infections. The language “purine” or “pyrimidine” includes the nitrogenous bases which are constituents of nucleic acids, co-enzymes, and nucleotides. The term “nucleotide” includes the basic structural units of nucleic acid molecules, which are comprised of a nitrogenous base, a pentose sugar (in the case of RNA, the sugar is ribose; in the case of DNA, the sugar is D-deoxyribose), and phosphoric acid. The language “nucleoside” includes molecules which serve as precursors to nucleotides, but which are lacking the phosphoric acid moiety that nucleotides possess. By inhibiting the biosynthesis of these molecules, or their mobilization to form nucleic acid molecules, it is possible to inhibit RNA and DNA synthesis; by inhibiting this activity in a fashion targeted to cancerous cells, the ability of tumor cells to divide and replicate may be inhibited. Additionally, there are nucleotides which do not form nucleic acid molecules, but rather serve as energy stores (i.e., AMP) or as coenzymes (i.e., FAD and NAD).

[0046] Several publications have described the use of these chemicals for these medical indications, by influencing purine and/or pyrimidine metabolism (e.g. Christopherson, R. I. and Lyons, S. D. (1990) “Potent inhibitors of de novo pyrimidine and purine biosynthesis as chemotherapeutic agents.” Med. Res. Reviews 10: 505-548). Studies of enzymes involved in purine and pyrimidine metabolism have been focused on the development of new drugs which can be used, for example, as immunosuppressants or anti-proliferants (Smith, J. L., (1995) “Enzymes in nucleotide synthesis.” Curr. Opin. Struct. Biol. 5: 752-757; (1995) Biochem Soc. Transact. 23: 877-902). However, purine and pyrimidine bases, nucleosides and nucleotides have other utilities: as intermediates in the biosynthesis of several fine chemicals (e.g., thiamine, S-adenosyl-methionine, folates, or riboflavin), as energy carriers for the cell (e.g., ATP or GTP), and for chemicals themselves, commonly used as flavor enhancers (e.g., IMP or GMP) or for several medicinal applications (see, for example, Kuninaka, A. (1996) Nucleotides and Related Compounds in Biotechnology vol. 6, Rehm et al., eds. VCH: Weinheim, p. 561-612). Also, enzymes involved in purine, pyrimidine, nucleoside, or nucleotide metabolism are increasingly serving as targets against which chemicals for crop protection, including fungicides, herbicides and insecticides, are developed.

[0047] The metabolism of these compounds in bacteria has been characterized (for reviews see, for example, Zalkin, H. and Dixon, J. E. (1992) “de novo purine nucleotide biosynthesis”, in: Progress in Nucleic Acid Research and Molecular Biology, vol. 42, Academic Press:, p. 259-287; and Michal, G. (1999) “Nucleotides and Nucleosides”, Chapter 8 in: Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology, Wiley: New York). Purine metabolism has been the subject of intensive research, and is essential to the normal functioning of the cell. Impaired purine metabolism in higher animals can cause severe disease, such as gout. Purine nucleotides are synthesized from ribose-5-phosphate, in a series of steps through the intermediate compound inosine-5′-phosphate (IMP), resulting in the production of guanosine-5′-monophosphate (GMP) or adenosine-5′-monophosphate (AMP), from which the triphosphate forms utilized as nucleotides are readily formed. These compounds are also utilized as energy stores, so their degradation provides energy for many different biochemical processes in the cell. Pyrimidine biosynthesis proceeds by the formation of uridine-5′-monophosphate (UMP) from ribose-5-phosphate. UMP, in turn, is converted to cytidine-5′-triphosphate (CTP). The deoxy-forms of all of these nucleotides are produced in a one step reduction reaction from the diphosphate ribose form of the nucleotide to the diphosphate deoxyribose form of the nucleotide. Upon phosphorylation, these molecules are able to participate in DNA synthesis.

[0048] D. Trehalose Metabolism and Uses

[0049] Trehalose consists of two glucose molecules, bound in α,α-1,1 linkage. It is commonly used in the food industry as a sweetener, an additive for dried or frozen foods, and in beverages. However, it also has applications in the pharmaceutical, cosmetics and biotechnology industries (see, for example, Nishimoto et al., (1998) U.S. Pat. No. 5,759,610; Singer, M. A. and Lindquist, S. (1998) Trends Biotech. 16: 460-467; Paiva, C. L. A. and Panek, A. D. (1996) Biotech. Ann. Rev. 2: 293-314; and Shiosaka, M. (1997) J. Japan 172: 97-102). Trehalose is produced by enzymes from many microorganisms and is naturally released into the surrounding medium, from which it can be collected using methods known in the art.

[0050] II. Elements and Methods of the Invention

[0051] The present invention is based, at least in part, on the discovery of novel molecules, referred to herein as MP nucleic acid and protein molecules (see Table 1), which play a role in or function in one or more cellular metabolic pathways. In one embodiment, the MP molecules catalyze an enzymatic reaction involving one or more amino acid, e.g., lysine or methionine, vitamin, cofactor, nutraceutical, nucleotide, nucleoside, or trehalose metabolic pathways. In a preferred embodiment, the activity of one or more MP molecules of the present invention, alone or in combination with molecules involved in the same or different metabolic pathway (e.g., methionine or lysine metabolism), in one or more C. glutamicum metabolic pathways for amino acids, vitamins, cofactors, nutraceuticals, nucleotides, nucleosides or trehalose has an impact on the production of a desired fine chemical by this organism. In a particularly preferred embodiment, the MP molecules of the invention are modulated in activity, such that the C. glutamicum metabolic pathways in which the MP proteins of the invention are involved are modulated in efficiency or output, which either directly or indirectly modulates the production or efficiency of production of a desired fine chemical by C. glutamicum. In a preferred embodiment, the fine chemical is an amino acid, e.g., lysine or methionine. In another preferred embodiment, the MP molecules are metZ, metY, and/or RXA00657 (see Table 1).

[0052] The language, “MP protein” or “MP polypeptide” includes proteins which play a role in, e.g., catalyze an enzymatic reaction, in one or more amino acid, vitamin, cofactor, nutraceutical, nucleotide, nucleoside or trehalose metabolic pathways. Examples of MP proteins include those encoded by the MP genes set forth in Table 1 and by the odd-numbered SEQ ID NOs. The terms “MP gene” or “MP nucleic acid sequence” include nucleic acid sequences encoding an MP protein, which consist of a coding region and also corresponding untranslated 5′ and 3′ sequence regions. Examples of MP genes include those set forth in Table 1. The terms “production” or “productivity” are art-recognized and include the concentration of the fermentation product (for example, the desired fine chemical) formed within a given time and a given fermentation volume (e.g., kg product per hour per liter). The term “efficiency of production” includes the time required for a particular level of production to be achieved (for example, how long it takes for the cell to attain a particular rate of output of a fine chemical). The term “yield” or “product/carbon yield” is art-recognized and includes the efficiency of the conversion of the carbon source into the product (i.e., fine chemical). This is generally written as, for example, kg product per kg carbon source. By increasing the yield or production of the compound, the quantity of recovered molecules, or of useful recovered molecules of that compound in a given amount of culture over a given amount of time is increased. The terms “biosynthesis” or a “biosynthetic pathway” are art-recognized and include the synthesis of a compound, preferably an organic compound, by a cell from intermediate compounds in what may be a multistep and highly regulated process. The terms “degradation” or a “degradation pathway” are art-recognized and include the breakdown of a compound, preferably an organic compound, by a cell to degradation products (generally speaking, smaller or less complex molecules) in what may be a multistep and highly regulated process. The language “metabolism” is art-recognized and includes the totality of the biochemical reactions that take place in an organism. The metabolism of a particular compound, then, (e.g., the metabolism of an amino acid such as glycine) comprises the overall biosynthetic, modification, and degradation pathways in the cell related to this compound.

[0053] The MP molecules of the present invention may be combined with one or more MP molecules of the invention or one or more molecules of the same or different metabolic pathway to increase the yield of a desired fine chemical. In a preferred embodiment, the fine chemical is an amino acid, e.g., lysine or methionine. Alternatively, or in addition, a byproduct which is not desired may be reduced by combination or disruption of MP molecules or other metabolic molecules (e.g., molecules involved in lysine or methionine metabolism). MP molecules combined with other molecules of the same or a different metabolic pathway may be altered in their nucleotide sequence and in the corresponding amino acid sequence to alter their activity under physiological conditions, which leads to an increase in productivity and/or yield of a desired fine chemical. In a further embodiment, an MP molecule in its original or in its above-described altered form may be combined with other molecules of the same or a different metabolic pathway which are altered in their nucleotide sequence in such a way that their activity is altered under physiological conditions which leads to an increase in productivity and/or yield of a desired fine chemical, e.g., an amino acid such as methionine or lysine.

[0054] In another embodiment, the MP molecules of the invention, alone or in combination with one or more molecules of the same or different metabolic pathway, are capable of modulating the production of a desired molecule, such as a fine chemical, in a microorganism such as C. glutamicum. Using recombinant genetic techniques, one or more of the biosynthetic or degradative enzymes of the invention for amino acids, e.g., lysine or methionine, vitamins, cofactors, nutraceuticals, nucleotides, nucleosides, or trehalose may be manipulated such that its function is modulated. For example, a biosynthetic enzyme may be improved in efficiency, or its allosteric control region destroyed such that feedback inhibition of production of the compound is prevented. Similarly, a degradative enzyme may be deleted or modified by substitution, deletion, or addition such that its degradative activity is lessened for the desired compound without impairing the viability of the cell. In each case, the overall yield or rate of production of one of these desired fine chemicals may be increased.

[0055] It is also possible that such alterations in the protein and nucleotide molecules of the invention may improve the production of other fine chemicals besides the amino acids, vitamins, cofactors, nutraceuticals, nucleotides, nucleosides, and trehalose. Metabolism of any one compound is necessarily intertwined with other biosynthetic and degradative pathways within the cell, and necessary cofactors, intermediates, or substrates in one pathway are likely supplied or limited by another such pathway. Therefore, by modulating the activity of one or more of the proteins of the invention, the production or efficiency of activity of another fine chemical biosynthetic or degradative pathway may be impacted. For example, amino acids serve as the structural units of all proteins, yet may be present intracellularly in levels which are limiting for protein synthesis; therefore, by increasing the efficiency of production or the yields of one or more amino acids within the cell, proteins, such as biosynthetic or degradative proteins, may be more readily synthesized. Likewise, an alteration in a metabolic pathway enzyme such that a particular side reaction becomes more or less favored may result in the over- or under-production of one or more compounds which are utilized as intermediates or substrates for the production of a desired fine chemical.

[0056] The isolated nucleic acid sequences of the invention are contained within the genome of a Corynebacterium glutamicum strain available through the American Type Culture Collection, given designation ATCC 13032. The nucleotide sequence of the isolated C. glutamicum MP DNAs and the predicted amino acid sequences of the C. glutamicum MP proteins are shown in the Sequence Listing as odd-numbered SEQ ID NOs and even-numbered SEQ ID NOs, respectively. Computational analyses were performed which classified and/or identified these nucleotide sequences as sequences which encode metabolic pathway proteins, e.g, proteins involved in the methionine or lysine metabolic pathways.

[0057] The present invention also pertains to proteins which have an amino acid sequence which is substantially homologous to an amino acid sequence of the invention (e.g., the sequence of an even-numbered SEQ ID NO of the Sequence Listing). As used herein, a protein which has an amino acid sequence which is substantially homologous to a selected amino acid sequence is least about 50% homologous to the selected amino acid sequence, e.g., the entire selected amino acid sequence. A protein which has an amino acid sequence which is substantially homologous to a selected amino acid sequence can also be least about 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, or 60%, preferably at least about 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, or 70%%, more preferably at least about 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, or 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, or 90%, or 91%, 92%, 93%, 94%, and even more preferably at least about 95%, 96%, 97%, 98%, 99%, 99.7% or more homologous to the selected amino acid sequence.

[0058] An MP protein of the invention, or a biologically active portion or fragment thereof, alone or in combination with one or more proteins of the same or different metabolic pathway, can catalyze an enzymatic reaction in one or more amino acid, vitamin, cofactor, nutraceutical, nucleotide, nucleoside, or trehalose metabolic pathways, or have one or more of the activities set forth in Table 1 (e.g., metabolism of methionine or lysine biosynthesis).

[0059] Various aspects of the invention are described in further detail in the following subsections:

[0060] A. Isolated Nucleic Acid Molecules

[0061] One aspect of the invention pertains to isolated nucleic acid molecules that encode MP polypeptides or biologically active portions thereof, as well as nucleic acid fragments sufficient for use as hybridization probes or primers for the identification or amplification of MP-encoding nucleic acid (e.g., MP DNA). As used herein, the term “nucleic acid molecule” is intended to include DNA molecules (e.g., cDNA or genomic DNA) and RNA molecules (e.g., mRNA) and analogs of the DNA or RNA generated using nucleotide analogs. This term also encompasses untranslated sequence located at both the 3′ and 5′ ends of the coding region of the gene: at least about 100 nucleotides of sequence upstream from the 5′ end of the coding region and at least about 20 nucleotides of sequence downstream from the 3′ end of the coding region of the gene. The nucleic acid molecule can be single-stranded or double-stranded, but preferably is double-stranded DNA. An “isolated” nucleic acid molecule is one which is separated from other nucleic acid molecules which are present in the natural source of the nucleic acid. Preferably, an “isolated” nucleic acid is free of sequences which naturally flank the nucleic acid (i.e., sequences located at the 5′ and 3′ ends of the nucleic acid) in the genomic DNA of the organism from which the nucleic acid is derived. For example, in various embodiments, the isolated MP nucleic acid molecule can contain less than about 5 kb, 4 kb, 3 kb, 2 kb, 1 kb, 0.5 kb or 0.1 kb of nucleotide sequences which naturally flank the nucleic acid molecule in genomic DNA of the cell from which the nucleic acid is derived (e.g, a C. glutamicum cell). Moreover, an “isolated” nucleic acid molecule, such as a DNA molecule, can be substantially free of other cellular material, or culture medium when produced by recombinant techniques, or chemical precursors or other chemicals when chemically synthesized.

[0062] A nucleic acid molecule of the present invention, e.g., a nucleic acid molecule having a nucleotide sequence of an odd-numbered SEQ ID NO of the Sequence Listing, or a portion thereof, can be isolated using standard molecular biology techniques and the sequence information provided herein. For example, a C. glutamicum MP DNA can be isolated from a C. glutamicum library using all or portion of one of the odd-numbered SEQ ID NO sequences of the Sequence Listing as a hybridization probe and standard hybridization techniques (e.g., as described in Sambrook, J., Fritsh, E. F., and Maniatis, T. Molecular Cloning.: A Laboratory Manual. 2nd, ed., Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1989). Moreover, a nucleic acid molecule encompassing all or a portion of one of the nucleic acid sequences of the invention (e.g., an odd-numbered SEQ ID NO:) can be isolated by the polymerase chain reaction using oligonucleotide primers designed based upon this sequence (e.g., a nucleic acid molecule encompassing all or a portion of one of the nucleic acid sequences of the invention (e.g., an odd-numbered SEQ ID NO of the Sequence Listing) can be isolated by the polymerase chain reaction using oligonucleotide primers designed based upon this same sequence). For example, mRNA can be isolated from normal endothelial cells (e.g., by the guanidinium-thiocyanate extraction procedure of Chirgwin et al. (1979) Biochemistry 18: 5294-5299) and DNA can be prepared using reverse transcriptase (e.g., Moloney MLV reverse transcriptase, available from Gibco/BRL, Bethesda, Md.; or AMV reverse transcriptase, available from Seikagaku America, Inc., St. Petersburg, Fla.). Synthetic oligonucleotide primers for polymerase chain reaction amplification can be designed based upon one of the nucleotide sequences shown in the Sequence Listing. A nucleic acid of the invention can be amplified using cDNA or, alternatively, genomic DNA, as a template and appropriate oligonucleotide primers according to standard PCR amplification techniques. The nucleic acid so amplified can be cloned into an appropriate vector and characterized by DNA sequence analysis. Furthermore, oligonucleotides corresponding to an MP nucleotide sequence can be prepared by standard synthetic techniques, e.g., using an automated DNA synthesizer.

[0063] In a preferred embodiment, an isolated nucleic acid molecule of the invention comprises one of the nucleotide sequences shown in the Sequence Listing. The nucleic acid sequences of the invention, as set forth in the Sequence Listing, correspond to the Corynebacterium glutamicum MP DNAs of the invention. This DNA comprises sequences encoding MP proteins (i.e., the “coding region”, indicated in each odd-numbered SEQ ID NO: sequence in the Sequence Listing), as well as 5′ untranslated sequences and 3′ untranslated sequences, also indicated in each odd-numbered SEQ ID NO: in the Sequence Listing. Alternatively, the nucleic acid molecule can comprise only the coding region of any of the nucleic acid sequences of the Sequence Listing.

[0064] For the purposes of this application, it will be understood that some of the MP nucleic acid and amino acid sequences set forth in the Sequence Listing have an identifying RXA, RXN, RXS, or RXC number having the designation “RXA”, “RXN”, “RXS”, or “RXC” followed by 5 digits (i.e., RXA, RXN, RXS, or RXC). Each of the nucleic acid sequences comprises up to three parts: a 5′ upstream region, a coding region, and a downstream region. Each of these three regions is identified by the same RXA, RXN, RXS, or RXC designation to eliminate confusion. The recitation “one of the odd-numbered sequences of the Sequence Listing”, then, refers to any of the nucleic acid sequences in the Sequence Listing, which may also be distinguished by their differing RXA, RXN, RXS, or RXC designations. The coding region of each of these sequences is translated into a corresponding amino acid sequence, which is also set forth in the Sequence Listing, as an even-numbered SEQ ID NO: immediately following the corresponding nucleic acid sequence. For example, the coding region for RXA00115 is set forth in SEQ ID NO:69, while the amino acid sequence which it encodes is set forth as SEQ ID NO:70. The sequences of the nucleic acid molecules of the invention are identified by the same RXA, RXN, RXS, or RXC designations as the amino acid molecules which they encode, such that they can be readily correlated. For example, the amino acid sequences designated RXA00115, RXN00403, and RXS03158 are translations of the coding regions of the nucleotide sequences of nucleic acid molecules RXA00115, RXN00403, and RXS03158, respectively. The correspondence between the RXA, RXN, RXS, and RXC nucleotide and amino acid sequences of the invention and their assigned SEQ ID NOs is set forth in Table 1.

[0065] Several of the genes of the invention- are “F-designated genes”. An F-designated gene includes those genes set forth in Table 1 which have an ‘F’ in front of the RXA, RXN, RXS, or RXC designation. For example, SEQ ID NO:77, designated, as indicated on Table 1, as “F RXA00254”, is an F-designated gene.

[0066] Also listed on Table 1 are the metZ (or metY) and metC genes (designated as SEQ ID NO: 1 and SEQ ID NO:3, respectively. The corresponding amino acid sequence encoded by the metZ and metC genes are designated as SEQ ID NO:2 and SEQ ID NO:5, respectively.

[0067] In one embodiment, the nucleic acid molecules of the present invention are not intended to include those compiled in Table 2.

[0068] In another preferred embodiment, an isolated nucleic acid molecule of the invention comprises a nucleic acid molecule which is a complement of one of the nucleotide sequences of the invention (e.g., a sequence of an odd-numbered SEQ ID NO: of the Sequence Listing), or a portion thereof. A nucleic acid molecule which is complementary to one of the nucleotide sequences of the invention is one which is sufficiently complementary to one of the nucleotide sequences shown in the Sequence Listing (e.g., the sequence of an odd-numbered SEQ ID NO:) such that it can hybridize to one of the nucleotide sequences of the invention, thereby forming a stable duplex.

[0069] In still another preferred embodiment, an isolated nucleic acid molecule of the invention comprises a nucleotide sequence which is at least about 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, or 60%, preferably at least about 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, or 70%%, more preferably at least about 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, or 80%, 81%, 82%, 83%, 84%, 85%, 86% 87%, 88%, 89%, or 90%, or 91%, 92%, 93%, 94%, and even more preferably at least about 95%, 96%, 97%, 98%, 99%, 99.7% or more homologous to a nucleotide sequence of the invention (e.g., a sequence of an odd-numbered SEQ ID NO: of the Sequence Listing), or a portion thereof. Ranges and identity values intermediate to the above-recited ranges, (e.g., 70-90% identical or 80-95% identical) are also intended to be encompassed by the present invention. For example, ranges of identity values using a combination of any of the above values recited as upper and/or lower limits are intended to be included. In an additional preferred embodiment, an isolated nucleic acid molecule of the invention comprises a nucleotide sequence which hybridizes, e.g., hybridizes under stringent conditions, to one of the nucleotide sequences of the invention, or a portion thereof.

[0070] Moreover, the nucleic acid molecule of the invention can comprise only a portion of the coding region of the sequence of one of the odd-numbered SEQ ID NOs of the Sequence Listing, for example a fragment which can be used as a probe or primer or a fragment encoding a biologically active portion of an MP protein. The nucleotide sequences determined from the cloning of the MP genes from C. glutamicum allows for the generation of probes and primers designed for use in identifying and/or cloning MP homologues in other cell types and organisms, as well as MP homologues from other Corynebacteria or related species. The probe/primer typically comprises substantially purified oligonucleotide. The oligonucleotide typically comprises a region of nucleotide sequence that hybridizes under stringent conditions to at least about 12, preferably about 25, more preferably about 40, 50 or 75 consecutive nucleotides of a sense strand of one of the nucleotide sequences of the invention (e.g., a sequence of one of the odd-numbered SEQ ID NOs of the Sequence Listing), an anti-sense sequence of one of these sequences, or naturally occurring mutants thereof. Primers based on a nucleotide sequence of the invention can be used in PCR reactions to clone MP homologues. Probes based on the MP nucleotide sequences can be used to detect transcripts or genomic sequences encoding the same or homologous proteins. In preferred embodiments, the probe further comprises a label group attached thereto, e.g. the label group can be a radioisotope, a fluorescent compound, an enzyme, or an enzyme cofactor. Such probes can be used as a part of a diagnostic test kit for identifying cells which misexpress an MP protein, such as by measuring a level of an MP-encoding nucleic acid in a sample of cells from a subject e.g., detecting MP mRNA levels or determining whether a genomic MP gene has been mutated or deleted.

[0071] In one embodiment, the nucleic acid molecule of the invention encodes a protein or portion thereof which includes an amino acid sequence which is sufficiently homologous to an amino acid sequence of the invention (e.g., a sequence of an even-numbered SEQ ID NO of the Sequence Listing) such that the protein or portion thereof maintains the ability to catalyze an enzymatic reaction in an amino acid, vitamin, cofactor, nutraceutical, nucleotide, nucleoside, or trehalose metabolic pathway. As used herein, the language “sufficiently homologous” refers to proteins or portions thereof which have amino acid sequences which include a minimum number of identical or equivalent (e.g., an amino acid residue which has a similar side chain as an amino acid residue in a sequence of one of the even-numbered SEQ ID NOs of the Sequence Listing) amino acid residues to an amino acid sequence of the invention such that the protein or portion thereof is able to catalyze an enzymatic reaction in a C. glutamicum amino acid, vitamin, cofactor, nutraceutical, nucleotide, nucleoside or trehalose metabolic pathway. Protein members of such metabolic pathways, as described herein, function to catalyze the biosynthesis or degradation of one or more of: amino acids, vitamins, cofactors, nutraceuticals, nucleotides, nucleosides, or trehalose. Examples of such activities are also described herein. Thus, “the function of an MP protein” contributes to the overall functioning of one or more such metabolic pathway and contributes, either directly or indirectly, to the yield, production, and/or efficiency of production of one or more fine chemicals. Examples of MP protein activities are set forth in Table 1.

[0072] In another embodiment, the protein is at least about 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, or 60%, preferably at least about 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, or 70%%, more preferably at least about 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, or 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, or 90%, or 91%, 92%, 93%, 94%, and even more preferably at least about 95%, 96%, 97%, 98%, 99%, 99.7% or more homologous to an entire amino acid sequence of the invention (e.g., a sequence of an even-numbered SEQ ID NO: of the Sequence Listing).

[0073] Portions of proteins encoded by the MP nucleic acid molecules of the invention are preferably biologically active portions of one of the MP proteins. As used herein, the term “biologically active portion of an MP protein” is intended to include a portion, e.g., a domain/motif, of an MP protein that catalyzes an enzymatic reaction in one or more C. glutamicum amino acid, vitamin, cofactor, nutraceutical, nucleotide, nucleoside, or trehalose metabolic pathways, or has an activity as set forth in Table 1. To determine whether an MP protein or a biologically active portion thereof can catalyze an enzymatic reaction in an amino acid, vitamin, cofactor, nutraceutical, nucleotide, nucleoside, or trehalose metabolic pathway, an assay of enzymatic activity may be performed. Such assay methods are well known to those of ordinary skill in the art, as detailed in Example 8 of the Exemplification.

[0074] Additional nucleic acid fragments encoding biologically active portions of an MP protein can be prepared by isolating a portion of one of the amino acid sequences of the invention (e.g., a sequence of an even-numbered SEQ ID NO: of the Sequence Listing), expressing the encoded portion of the MP protein or peptide (e.g., by recombinant expression in vitro) and assessing the activity of the encoded portion of the MP protein or peptide.

[0075] The invention further encompasses nucleic acid molecules that differ from one of the nucleotide sequences of the invention (e.g., a sequence of an odd-numbered SEQ ID NO: of the Sequence Listing) (and portions thereof) due to degeneracy of the genetic code and thus encode the same MP protein as that encoded by the nucleotide sequences of the invention. In another embodiment, an isolated nucleic acid molecule of the invention has a nucleotide sequence encoding a protein having an amino acid sequence shown in the Sequence Listing (e.g., an even-numbered SEQ ID NO:). In a still further embodiment, the nucleic acid molecule of the invention encodes a full length C. glutamicum protein which is substantially homologous to an amino acid sequence of the invention (encoded by an open reading frame shown in an odd-numbered SEQ ID NO: of the Sequence Listing).

[0076] It will be understood by one of ordinary skill in the art that in one embodiment the sequences of the invention are not meant to include the sequences of the prior art, such as those Genbank sequences set forth in Table 2, which was available prior to the present invention. In one embodiment, the invention includes nucleotide and amino acid sequences having a percent identity to a nucleotide or amino acid sequence of the invention which is greater than that of a sequence of the prior art (e.g., a Genbank sequence (or the protein encoded by such a sequence) set forth in Table 2). For example, the invention includes a nucleotide sequence which is greater than and/or at least 45% identical to the nucleotide sequence designated RXA00657 SEQ ID NO:5 One of ordinary skill in the art would be able to calculate the lower threshold of percent identity for any given sequence of the invention by examining the GAP-calculated percent identity scores set forth in Table 4 for each of the three top hits for the given sequence, and by subtracting the highest GAP-calculated percent identity from 100 percent. One of ordinary skill in the art will also appreciate that nucleic acid and amino acid sequences having percent identities greater than the lower threshold so calculated (e.g., at least about 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, or 60preferably at least about 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, or 70%, more preferably at least about 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, or 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, or 90%, or 91%, 92%, 93%, 94%, and even more preferably at least about 95%, 96%, 97%, 98%, 99%, 99.7% or more identical) are also encompassed by the invention.

[0077] In addition to the C. glutamicum MP nucleotide sequences set forth in the Sequence Listing as odd-numbered SEQ ID NOs, it will be appreciated by one of ordinary skill in the art that DNA sequence polymorphisms that lead to changes in the amino acid sequences of MP proteins may exist within a population (e.g., the C. glutamicum population). Such genetic polymorphism in the MP gene may exist among individuals within a population due to natural variation. As used herein, the terms “gene” and “recombinant gene” refer to nucleic acid molecules comprising an open reading frame encoding an MP protein, preferably a C. glutamicum MP protein. Such natural variations can typically result in 1-5% variance in the nucleotide sequence of the MP gene. Any and all such nucleotide variations and resulting amino acid polymorphisms in MP that are the result of natural variation and that do not alter the functional activity of MP proteins are intended to be within the scope of the invention.

[0078] Nucleic acid molecules corresponding to natural variants and non-C. glutamicum homologues of the C. glutamicum MP DNA of the invention can be isolated based on their homology to the C. glutamicum MP nucleic acid disclosed herein using the C. glutamicum DNA, or a portion thereof, as a hybridization probe according to standard hybridization techniques under stringent hybridization conditions. Accordingly, in another embodiment, an isolated nucleic acid molecule of the invention is at least 15 nucleotides in length and hybridizes under stringent conditions to the nucleic acid molecule comprising a nucleotide sequence of an odd-numbered SEQ ID NO: of the Sequence Listing. In other embodiments, the nucleic acid is at least 30, 50, 100, 250 or more nucleotides in length. As used herein, the term “hybridizes under stringent conditions” is intended to describe conditions for hybridization and washing under which nucleotide sequences at least 60% homologous to each other typically remain hybridized to each other. Preferably, the conditions are such that sequences at least about 65%, more preferably at least about 70%, and even more preferably at least about 75% or more homologous to each other typically remain hybridized to each other. Such stringent conditions are known to one of ordinary skill in the art and can be found in Current Protocols in Molecular Biology, John Wiley & Sons, N.Y. (1989), 6.3.1-6.3.6. A preferred, non-limiting example of stringent hybridization conditions are hybridization in 6×sodium chloride/sodium citrate (SSC) at about 45° C., followed by one or more washes in 0.2×SSC, 0.1% SDS at 50-65° C. Preferably, an isolated nucleic acid molecule of the invention that hybridizes under stringent conditions to a nucleotide sequence of the invention corresponds to a naturally-occurring nucleic acid molecule. As used herein, a “naturally-occurring” nucleic acid molecule refers to an RNA or DNA molecule having a nucleotide sequence that occurs in nature (e.g., encodes a natural protein). In one embodiment, the nucleic acid encodes a natural C. glutamicum MP protein.

[0079] In addition to naturally-occurring variants of the MP sequence that may exist in the population, one of ordinary skill in the art will further appreciate that changes can be introduced by mutation into a nucleotide sequence of the invention, thereby leading to changes in the amino acid sequence of the encoded MP protein, without altering the functional ability of the MP protein. For example, nucleotide substitutions leading to amino acid substitutions at “non-essential” amino acid residues can be made in a nucleotide sequence of the invention. A “non-essential” amino acid residue is a residue that can be altered from the wild-type sequence of one of the MP proteins (e.g., an even-numbered SEQ ID NO: of the Sequence Listing) without altering the activity of said MP protein, whereas an “essential” amino acid residue is required for MP protein activity. Other amino acid residues, however, (e.g., those that are not conserved or only semi-conserved in the domain having MP activity) may not be essential for activity and thus are likely to be amenable to alteration without altering MP activity.

[0080] Accordingly, another aspect of the invention pertains to nucleic acid molecules encoding MP proteins that contain changes in amino acid residues that are not essential for MP activity. Such MP proteins differ in amino acid sequence from a sequence of an even-numbered SEQ ID NO: of the Sequence Listing yet retain at least one of the MP activities described herein. In one embodiment, the isolated nucleic acid molecule comprises a nucleotide sequence encoding a protein, wherein the protein comprises an amino acid sequence at least about 50% homologous to an amino acid sequence of the invention and is capable of catalyzing an enzymatic reaction in an amino acid, vitamin, cofactor, nutraceutical, nucleotide, nucleoside, or trehalose metabolic pathway, or has one or more activities set forth in Table 1. Preferably, the protein encoded by the nucleic acid molecule is at least about 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, or 60%, preferably at least about 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, or 70%%, more preferably at least about 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, or 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, or 90%, or 91%, 92%, 93%, 94%, and even more preferably at least about 95%, 96%, 97%, 98%, 99%, 99.7% homologous to one of the amino acid sequences of the invention.

[0081] To determine the percent homology of two amino acid sequences (e.g., one of the amino acid sequences of the invention and a mutant form thereof) or of two nucleic acids, the sequences are aligned for optimal comparison purposes (e.g., gaps can be introduced in the sequence of one protein or nucleic acid for optimal alignment with the other protein or nucleic acid). The amino acid residues or nucleotides at corresponding amino acid positions or nucleotide positions are then compared. When a position in one sequence (e.g., one of the amino acid sequences of the invention) is occupied by the same amino acid residue or nucleotide as the corresponding position in the other sequence (e.g., a mutant form of the amino acid sequence), then the molecules are homologous at that position (i. e., as used herein amino acid or nucleic acid “homology” is equivalent to amino acid or nucleic acid “identity”). The percent homology between the two sequences is a function of the number of identical positions shared by the sequences (i.e., % homology=# of identical positions/total # of positions×100).

[0082] An isolated nucleic acid molecule encoding an MP protein homologous to a protein sequence of the invention (e.g., a sequence of an even-numbered SEQ ID NO: of the Sequence Listing) can be created by introducing one or more nucleotide substitutions, additions or deletions into a nucleotide sequence of the invention such that one or more amino acid substitutions, additions or deletions are introduced into the encoded protein. Mutations can be introduced into one of the nucleotide sequences of the invention by standard techniques, such as site-directed mutagenesis and PCR-mediated mutagenesis. Preferably, conservative amino acid substitutions are made at one or more predicted non-essential amino acid residues. A “conservative amino acid substitution” is one in which the amino acid residue is replaced with an amino acid residue having a similar side chain. Families of amino acid residues having similar side chains have been defined in the art. These families include amino acids with basic side chains (e.g., lysine, arginine, histidine), acidic side chains (e.g., aspartic acid, glutamic acid), uncharged polar side chains (e.g., glycine, asparagine, glutamine, serine, threonine, tyrosine, cysteine), nonpolar side chains (e.g, alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, tryptophan), beta-branched side chains (e.g., threonine, valine, isoleucine) and aromatic side chains (e.g., tyrosine, phenylalanine, tryptophan, histidine). Thus, a predicted nonessential amino acid residue in an MP protein is preferably replaced with another amino acid residue from the same side chain family. Alternatively, in another embodiment, mutations can be introduced randomly along all or part of an MP coding sequence, such as by saturation mutagenesis, and the resultant mutants can be screened for an MP activity described herein to identify mutants that retain MP activity. Following mutagenesis of the nucleotide sequence of one of the odd-numbered SEQ ID NOs of the Sequence Listing, the encoded protein can be expressed recombinantly and the activity of the protein can be determined using, for example, assays described herein (see Example 8 of the Exemplification).

[0083] In addition to the nucleic acid molecules encoding MP proteins described above, another aspect of the invention pertains to isolated nucleic acid molecules which are antisense thereto. An “antisense” nucleic acid comprises a nucleotide sequence which is complementary to a “sense” nucleic acid encoding a protein, e.g., complementary to the coding strand of a double-stranded DNA molecule or complementary to an mRNA sequence. Accordingly, an antisense nucleic acid can hydrogen bond to a sense nucleic acid. The antisense nucleic acid can be complementary to an entire MP coding strand, or to only a portion thereof. In one embodiment, an antisense nucleic acid molecule is antisense to a “coding region” of the coding strand of a nucleotide sequence encoding an MP protein. The term “coding region” refers to the region of the nucleotide sequence comprising codons which are translated into amino acid residues (e.g., the entire coding region of SEQ ID NO.:1 (metZ) comprises nucleotides 363 to 1673). In another embodiment, the antisense nucleic acid molecule is antisense to a “noncoding region” of the coding strand of a nucleotide sequence encoding MP. The term “noncoding region” refers to 5′ and 3′ sequences which flank the coding region that are not translated into amino acids (i.e., also referred to as 5′ and 3′ untranslated regions).

[0084] Given the coding strand sequences encoding MP disclosed herein (e.g., the sequences set forth as odd-numbered SEQ ID NOs in the Sequence Listing), antisense nucleic acids of the invention can be designed according to the rules of Watson and Crick base pairing. The antisense nucleic acid molecule can be complementary to the entire coding region of MP mRNA, but more preferably is an oligonucleotide which is antisense to only a portion of the coding or noncoding region of MP mRNA. For example, the antisense oligonucleotide can be complementary to the region surrounding the translation start site of MP mRNA. An antisense oligonucleotide can be, for example, about 5, 10, 15, 20, 25, 30, 35, 40, 45 or 50 nucleotides in length. An antisense nucleic acid of the invention can be constructed using chemical synthesis and enzymatic ligation reactions using procedures known in the art. For example, an antisense nucleic acid (e.g., an antisense oligonucleotide) can be chemically synthesized using naturally occurring nucleotides or variously modified nucleotides designed to increase the biological stability of the molecules or to increase the physical stability of the duplex formed between the antisense and sense nucleic acids, e.g., phosphorothioate derivatives and acridine substituted nucleotides can be used. Examples of modified nucleotides which can be used to generate the antisense nucleic acid include 5-fluorouracil, 5-bromouracil, 5-chlorouracil, 5-iodouracil, hypoxanthine, xanthine, 4-acetylcytosine, 5-(carboxyhydroxylmethyl) uracil, 5-carboxymethylaminomethyl-2-thiouridine, 5-carboxymethylaminomethyluracil, dihydrouracil, beta-D-galactosylquenosine, inosine, N6-isopentenyladenine, 1-methylguanine, 1-methylinosine, 2,2-dimethylguanine, 2-methyladenine, 2-methylguanine, 3-methylcytosine, 5-methylcytosine, N6-adenine, 7-methylguanine, 5-methylaminomethyluracil, 5-methoxyaminomethyl-2-thiouracil, beta-D-mannosylqueosine, 5′-methoxycarboxymethyluracil, 5-methoxyuracil, 2-methylthio-N6-isopentenyladenine, uracil-5-oxyacetic acid (v), wybutoxosine, pseudouracil, queosine, 2-thiocytosine, 5-methyl-2-thiouracil, 2-thiouracil, 4-thiouracil, 5-methyluracil, uracil-5-oxyacetic acid methylester, uracil-5-oxyacetic acid (v), 5-methyl-2-thiouracil, 3-(3-amino-3-N-2-carboxypropyl) uracil, (acp3)w, and 2,6-diaminopurine. Alternatively, the antisense nucleic acid can be produced biologically using an expression vector into which a nucleic acid has been subcloned in an antisense orientation (i.e., RNA transcribed from the inserted nucleic acid will be of an antisense orientation to a target nucleic acid of interest, described further in the following subsection).

[0085] The antisense nucleic acid molecules of the invention are typically administered to a cell or generated in situ such that they hybridize with or bind to cellular mRNA and/or genomic DNA encoding an MP protein to thereby inhibit expression of the protein, e.g., by inhibiting transcription and/or translation. The hybridization can be by conventional nucleotide complementarity to form a stable duplex, or, for example, in the case of an antisense nucleic acid molecule which binds to DNA duplexes, through specific interactions in the major groove of the double helix. The antisense molecule can be modified such that it specifically binds to a receptor or an antigen expressed on a selected cell surface, e.g., by linking the antisense nucleic acid molecule to a peptide or an antibody which binds to a cell surface receptor or antigen. The antisense nucleic acid molecule can also be delivered to cells using the vectors described herein. To achieve sufficient intracellular concentrations of the antisense molecules, vector constructs in which the antisense nucleic acid molecule is placed under the control of a strong prokaryotic, viral, or eukaryotic promoter are preferred.

[0086] In yet another embodiment, the antisense nucleic acid molecule of the invention is an α-anomeric nucleic acid molecule. An α-anomeric nucleic acid molecule forms specific double-stranded hybrids with complementary RNA in which, contrary to the usual β-units, the strands run parallel to each other (Gaultier et al. (1987) Nucleic Acids. Res. 15:6625-6641). The antisense nucleic acid molecule can also comprise a 2′-o-methylribonucleotide (Inoue et al. (1987) Nucleic Acids Res. 15:6131-6148) or a chimeric RNA-DNA analogue (Inoue et al. (1987) FEBS Lett. 215:327-330).

[0087] In still another embodiment, an antisense nucleic acid of the invention is a ribozyme. Ribozymes are catalytic RNA molecules with ribonuclease activity which are capable of cleaving a single-stranded nucleic acid, such as an mRNA, to which they have a complementary region. Thus, ribozymes (e.g., hammerhead ribozymes (described in Haselhoff and Gerlach (1988) Nature 334:585-591)) can be used to catalytically cleave MP mRNA transcripts to thereby inhibit translation of MP mRNA. A ribozyme having specificity for an MP-encoding nucleic acid can be designed based upon the nucleotide sequence of an MP DNA disclosed herein (i.e., SEQ ID NO:1 (metZ). For example, a derivative of a Tetrahymena L-19 IVS RNA can be constructed in which the nucleotide sequence of the active site is complementary to the nucleotide sequence to be cleaved in an MP-encoding mRNA. See, e.g., Cech et al. U.S. Pat. No. 4,987,071 and Cech et al. U.S. Pat. No. 5,116,742. Alternatively, MP mRNA can be used to select a catalytic RNA having a specific ribonuclease activity from a pool of RNA molecules. See, e.g., Bartel, D. and Szostak, J. W. (1993) Science 261:1411-1418.

[0088] Alternatively, MP gene expression can be inhibited by targeting nucleotide sequences complementary to the regulatory region of an MP nucleotide sequence (e.g., an MP promoter and/or enhancers) to form triple helical structures that prevent transcription of an MP gene in target cells. See generally, Helene, C. (1991) Anticancer Drug Des. 6(6):569-84; Helene, C. et al. (1992) Ann. N.Y Acad. Sci. 660:27-36; and Maher, L. J. (1992) Bioassays 14(12):807-15.

[0089] Another aspect of the invention pertains to combinations of genes involved in methionine and/or lysine metabolism and the use of to combinations of genes involved in methionine and/or lysine metabolism in the methods of the invention. Preferred combinations are the combination of metZ with metC, metB (encoding Cystathionine-Synthase), metA (encoding homoserine-O-acetyltransferase), metE (encoding Methionine Synthase), metH (encoding Methionine Synthase), hom (encoding homoserine dehydrogenase), asd (encoding aspartatesemialdehyd dehydrogenase), lysC/ask (encoding aspartokinase) and rxa00657 (herein designated as SEQ ID NO.:5), dapA, (gene encoding DIHYDRODIPICOLINATE SYNTHASE), dapB (gene encoding DIHYDRODIPICOLINATE REDUCTASE), dapC (gene encoding 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase), dapD/argD (gene encoding acetylornithine transaminase), dapE (gene encoding succinyldiaminopimelate desuccinylase), dapF (gene encoding diaminopimelate epimerase), lysA (gene encoding diaminopimelate decarboxylase), ddh (gene encoding diaminopimelate dehydrogenase), lysE (gene encoding for the lysine exporter ), lysG (gene encoding for the exporter regulator), hsk (gene encoding homoserine kinase) as well as genes involved in anaplerotic reaction such as ppc (gene encoding phosphoenolpyruvate carboxylase), ppcK (gene encoding phosphoenolpyruvate carboxykinase), pycA (gene encoding pyruvate carboxylase), accD, accA, accB, accC (genes encoding for subunits of acetyl-CoA-carboxylase), as well as genes of the pentose-phosphate pathway, gpdh genes encoding glucose-6-phophate-dehydrogenase, opcA, pgdh (gene encoding 6-phosphogluconate-dehydrogenase), ta (gene encoding transaldolase), tk (gene encoding gene encoding transketolase), pgl (gene encoding 6-PHOSPHOGLUCONO-LACTONASE), rlpe (gene encoding RIBULOSE-PHOSPHATE 3-EPIMERASE) rpe (gene encoding RIBOSE 5-PHOSPHATE EPIMERASE) or combinations of the above-mentioned genes of the pentose-phosphate-pathways, or other MP genes of the invention.

[0090] The genes may be altered in their nucleotide sequence and in the corresponding amino acid sequence resulting in derivatives in such a way that their activity is altered under physiological conditions which leads to an increase in productivity and/or yield of a desired fine chemical, e.g., an amino acid such as methionine or lysine. One class of such alterations or derivatives is well known for the nucleotide sequence of the ask gene encoding aspartokinase. These alterations lead to removal of feed back inhibition by the amino acids lysine and threonine and subsequently to lysine overproduction. In a preferred embodiment the metZ gene or altered forms of the metZ gene are used in a Corynebacterium strain in combination with ask, hom, metA and metH or derivatives of these genes. In another preferred embodiment metZ or altered forms of the metZ gene are used in a Corynebacterium strain in combination with ask, hom, metA and metE or derivatives of these genes. In a more preferred embodiment, the gene combinations MetZ or altered forms of the metZ gene are combined with ask, hom, meta and metH or derivatives of these genes, or metZ is combined with ask, hom, metA and metE or derivatives of these genes in a Corynebacterium strain and sulfur sources such as sulfates, thiosulfates, sulfites and also more reduced sulfur sources such as H₂S and sulfides and derivatives are used in the growth medium. Also, sulfur sources such as methyl mercaptan, methanesulfonic acid, thioglycolates, thiocyanates, thiourea, sulfur containing amino acids such as cysteine and other sulfur containing compounds can be used. Another aspect of the invention pertains to the use of the above mentioned gene combinations in a Corynebacterium strain which is, before or after introduction of the genes, mutagenized by radiation or by mutagenic chemicals well-known to one of ordinary skill in the art and selected for resistance against high concentrations of the fine chemical of interest, e.g. lysine or methionine or analogues of the desired fine chemical such as the methionine analogues ethionine, methyl methionine, or others. In another embodiment, the gene combinations mentioned above can be expressed in a Corynebacterium strain having particular gene disruptions. Preferred are gene disruptions that encode proteins that favor carbon flux to undesired metabolites. Where methionine is the desired fine chemical the formation of lysine may be unfavorable. In such a case the combination of the above mentioned genes should proceed in a Corynebacterium strain bearing a gene disruption of the lysA gene (encoding diaminopimelate decarboxylase) or the ddh gene (encoding the meso-diaminopimelate dehydrogenase catalysing the conversion of tetrahydropicolinate to meso-diaominopimelate). In a preferred embodiment, a favorable combination of the above-mentioned genes are all altered in such a way that their gene products are not feed back inhibited by end products or metabolites of the biosynthetic pathway leading to the desired fine chemical. In the case that the desired fine chemical is methionine, the gene combinations may be expressed in a strain previously treated with mutagenic agents or radiation and selected for the above-mentioned resistance. Additionally, the strain should be grown in a growth medium containing one or more of the above mentioned sulfur sources.

[0091] In another embodiment of the invention, a gene was identified from the genome of Corynebacterium glutamicum as a gene coding for a hypothetical transcriptional regulatory protein. This gene is described as RXA00657. The nucleotide sequence of RXA00657 corresponds to SEQ ID NO:5. The amino acid sequence of RXA00657 corresponds to SEQ ID NO:6. It was found that when the RXA00657 gene, as well as upstream and downstream regulatory regions described in the examples, was cloned into a vector capable of replicating in Corynebacterium glutamicum and transformed and expressed in a lysine producing strain such as ATCC13286, that this strain produced more lysine compared to the strain transformed with the same plasmid lacking the aforementioned nucleotide fragment RXA00657. In addition to the observation that the lysine titer was increased in the mentioned strain, the selectivity determined by the molar amount of lysine produced compared to the molar amount of sucrose consumed was increased (see Example 14). Overexpression of RXA00657 in combination with the overexpression of other genes either directly involved in the lysine specific pathway such as lysC, dapA, dapB, dapC, dapD, dapF, ddh, lysE, lysG, and lysR results in an increase in the production of lysine compared to RXA00657 alone.

[0092] B. Recombinant Expression Vectors and Host Cells

[0093] Another aspect of the invention pertains to vectors, preferably expression vectors, containing a nucleic acid encoding an MP protein (or a portion thereof) or combinations of genes wherein at least one gene encodes for an MP protein. As used herein, the term “vector” refers to a nucleic acid molecule capable of transporting another nucleic acid to which it has been linked. One type of vector is a “plasmid”, which refers to a circular double stranded DNA loop into which additional DNA segments can be ligated. Another type of vector is a viral vector, wherein additional DNA segments can be ligated into the viral genome. Certain vectors are capable of autonomous replication in a host cell into which they are introduced (e.g., bacterial vectors having a bacterial origin of replication and episomal mammalian vectors). Other vectors (e.g., non-episomal mammalian vectors) are integrated into the genome of a host cell upon introduction into the host cell, and thereby are replicated along with the host genome. Moreover, certain vectors are capable of directing the expression of genes to which they are operatively linked. Such vectors are referred to herein as “expression vectors”. In general, expression vectors of utility in recombinant DNA techniques are often in the form of plasmids. In the present specification, “plasmid” and “vector” can be used interchangeably as the plasmid is the most commonly used form of vector. However, the invention is intended to include such other forms of expression vectors, such as viral vectors (e.g., replication defective retroviruses, adenoviruses and adeno-associated viruses), which serve equivalent functions.

[0094] The recombinant expression vectors of the invention comprise a nucleic acid of the invention in a form suitable for expression of the nucleic acid in a host cell, which means that the recombinant expression vectors include one or more regulatory sequences, selected on the basis of the host cells to be used for expression, which is operatively linked to the nucleic acid sequence to be expressed. Within a recombinant expression vector, “operably linked” is intended to mean that the nucleotide sequence of interest is linked to the regulatory sequence(s) in a manner which allows for expression of the nucleotide sequence (e.g., in an in vitro transcription/translation system or in a host cell when the vector is introduced into the host cell). The term “regulatory sequence” is intended to include promoters, repressor binding sites, activator binding sites, enhancers and other expression control elements (e.g., terminators, polyadenylation signals, or other elements of mRNA secondary structure). Such regulatory sequences are described, for example, in Goeddel; Gene Expression Technology: Methods in Enzymology 185, Academic Press, San Diego, Calif. (1990). Regulatory sequences include those which direct constitutive expression of a nucleotide sequence in many types of host cell and those which direct expression of the nucleotide sequence only in certain host cells. Preferred regulatory sequences are, for example, promoters such as cos-, tac-, trp-, tet-, trp-tet-, lpp-, lac-, lpp-lac-, lacI^(q)-, T7-, T5-, T3-, gal-, trc-, ara-, SP6-, arny, SPO2, λ-P_(R)- or λP_(L), which are used preferably in bacteria. Additional regulatory sequences are, for example, promoters from yeasts and fungi, such as ADC1, MFα, AC, P-60, CYC1, GAPDH, TEF, rp28, ADH, promoters from plants such as CaMV/35S, SSU, OCS, lib4, usp, STLS1, B33, nos or ubiquitin- or phaseolin-promoters. It is also possible to use artificial promoters. It will be appreciated by one of ordinary skill in the art that the design of the expression vector can depend on such factors as the choice of the host cell to be transformed, the level of expression of protein desired, etc. The expression vectors of the invention can be introduced into host cells to thereby produce proteins or peptides, including fusion proteins or peptides, encoded by nucleic acids as described herein (e.g., MP proteins, mutant forms of MP proteins, fusion proteins, etc.).

[0095] The recombinant expression vectors of the invention can be designed for expression of MP proteins in prokaryotic or eukaryotic cells. For example, MP genes can be expressed in bacterial cells such as C. glutamicum, insect cells (using baculovirus expression vectors), yeast and other fungal cells (see Romanos, M. A. et al. (1992) “Foreign gene expression in yeast: a review”, Yeast 8: 423-488; van den Hondel, C.A.M.J.J. et al. (1991) “Heterologous gene expression in filamentous fungi” in: More Gene Manipulations in Fungi, J. W. Bennet & L. L. Lasure, eds., p. 396-428: Academic Press: San Diego; and van den Hondel, C.A.M.J.J. & Punt, P. J. (1991) “Gene transfer systems and vector development for filamentous fungi, in: Applied Molecular Genetics of Fungi, Peberdy, J. F. et al., eds., p. 1-28, Cambridge University Press: Cambridge), algae and multicellular plant cells (see Schmidt, R. and Willmitzer, L. (1988) High efficiency Agrobacterium tumefaciens—mediated transformation of Arabidopsis thaliana leaf and cotyledon explants” Plant Cell Rep.: 583-586), or mammalian cells. Suitable host cells are discussed further in Goeddel, Gene Expression Technology: Methods in Enzymology 185, Academic Press, San Diego, Calif. (1990). Alternatively, the recombinant expression vector can be transcribed and translated in vitro, for example using T7 promoter regulatory sequences and T7 polymerase.

[0096] Expression of proteins in prokaryotes is most often carried out with vectors containing constitutive or inducible promoters directing the expression of either fusion or non-fusion proteins. Fusion vectors add a number of amino acids to a protein encoded therein, usually to the amino terminus of the recombinant protein but also to the C-terminus or fused within suitable regions in the proteins. Such fusion vectors typically serve three purposes: 1) to increase expression of recombinant protein; 2) to increase the solubility of the recombinant protein; and 3) to aid in the purification of the recombinant protein by acting as a ligand in affinity purification. Often, in fusion expression vectors, a proteolytic cleavage site is introduced at the junction of the fusion moiety and the recombinant protein to enable separation of the recombinant protein from the fusion moiety subsequent to purification of the fusion protein. Such enzymes, and their cognate recognition sequences, include Factor Xa, thrombin and enterokinase.

[0097] Typical fusion expression vectors include pGEX (Pharmacia Biotech Inc; Smith, D. B. and Johnson, K. S. (1988) Gene 67:31-40), pMAL (New England Biolabs, Beverly, Mass.) and pRIT5 (Pharmacia, Piscataway, N.J.) which fuse glutathione S-transferase (GST), maltose E binding protein, or protein A, respectively, to the target recombinant protein. In one embodiment, the coding sequence of the MP protein is cloned into a pGEX expression vector to create a vector encoding a fusion protein comprising, from the N-terminus to the C-terminus, GST-thrombin cleavage site-X protein. The fusion protein can be purified by affinity chromatography using glutathione-agarose resin. Recombinant MP protein unfused to GST can be recovered by cleavage of the fusion protein with thrombin.

[0098] Examples of suitable inducible non-fusion E. coli expression vectors include pTrc (Amann et al., (1988) Gene 69:301-315) pLG338, pACYC184, pBR322, pUC18, pUC19, pKC30, pRep4, pHS1, pHS2, pPLc236, pMBL24, pLG200, pUR290, pIN-III113-B1, λgt11, pBdCl, and pET 11d (Studier et al., Gene Expression Technology: Methods in Enzymology 185, Academic Press, San Diego, Calif. (1990) 60-89; and Pouwels et al., eds. (1985) Cloning Vectors. Elsevier: New York IBSN 0 444 904018). Target gene expression from the pTrc vector relies on host RNA polymerase transcription from a hybrid trp-lac fusion promoter. Target gene expression from the pET 11d vector relies on transcription from a T7 gn10-lac fusion promoter mediated by a coexpressed viral RNA polymerase (T7 gn1). This viral polymerase is supplied by host strains BL21(DE3) or HMS174(DE3) from a resident λ prophage harboring a T7 gn1 gene under the transcriptional control of the lacUV 5 promoter. For transformation of other varieties of bacteria, appropriate vectors may be selected. For example, the plasmids pIJ101, pIJ364, pIJ702 and pIJ361 are known to be useful in transforming Streptomyces, while plasmids pUB110, pC194, or pBD214 are suited for transformation of Bacillus species. Several plasmids of use in the transfer of genetic information into Corynebacterium include pHM1519, pBL1, pSA77, or pAJ667 (Pouwels et al., eds. (1985) Cloning Vectors. Elsevier: New York IBSN 0 444 904018).

[0099] One strategy to maximize recombinant protein expression is to express the protein in a host bacteria with an impaired capacity to proteolytically cleave the recombinant protein (Gottesman, S., Gene Expression Technology: Methods in Enzymology 185, Academic Press, San Diego, Calif. (1990)119-128). Another strategy is to alter the nucleic acid sequence of the nucleic acid to be inserted into an expression vector so that the individual codons for each amino acid are those preferentially utilized in the bacterium chosen for expression, such as C. glutamicum (Wada et al. (1992) Nucleic Acids Res. 20:2111-2118). Such alteration of nucleic acid sequences of the invention can be carried out by standard DNA synthesis techniques.

[0100] In another embodiment, the MP protein expression vector is a yeast expression vector. Examples of vectors for expression in yeast S. cerevisiae include pYepSec1 (Baldari, et al., (1987) Embo J. 6:229-234),, 2μ, pAG-1, Yep6, Yep13, pEMBLYe23, pMFa (Kurjan and Herskowitz, (1982) Cell 30:933-943), pJRY88 (Schultz et al., (1987) Gene 54:113-123), and pYES2 (Invitrogen Corporation, San Diego, Calif.). Vectors and methods for the construction of vectors appropriate for use in other fungi, such as the filamentous fungi, include those detailed in: van den Hondel, C.A.M.J.J. & Punt, P. J. (1991) “Gene transfer systems and vector development for filamentous fungi, in: Applied Molecular Genetics of Fungi, J. F. Peberdy, et al., eds., p. 1-28, Cambridge University Press: Cambridge, and Pouwels et al, eds. (1985) Cloning Vectors. Elsevier: New York (IBSN 0 444 904018).

[0101] Alternatively, the MP proteins of the invention can be expressed in insect cells using baculovirus expression vectors. Baculovirus vectors available for expression of proteins in cultured insect cells (e.g., Sf 9 cells) include the pAc series (Smith et al. (1983) Mol. Cell Biol. 3:2156-2165) and the pVL series (Lucklow and Summers (1989) Virology 170:31-39).

[0102] In another embodiment, the MP proteins of the invention may be expressed in unicellular plant cells (such as algae) or in plant cells from higher plants (e.g., the spermatophytes, such as crop plants). Examples of plant expression vectors include those detailed in: Becker, D., Kemper, E., Schell, J. and Masterson, R. (1992) “New plant binary vectors with selectable markers located proximal to the left border”, Plant Mol. Biol. 20: 1195-1197; and Bevan, M. W. (1984) “Binary Agrobacterium vectors for plant transformation”, Nuc. Acid. Res. 12: 8711-8721, and include pLGV23, pGHlac+, pBIN19, pAK2004, and pDH51 (Pouwels et al., eds. (1985) Cloning Vectors. Elsevier: New York IBSN 0 444 904018).

[0103] In yet another embodiment, a nucleic acid of the invention is expressed in mammalian cells using a mammalian expression vector. Examples of mammalian expression vectors include pCDM8 (Seed, B. (1987) Nature 329:840) and pMT2PC (Kaufman et al. (1987) EMBO J. 6:187-195). When used in mammalian cells, the expression vector's control functions are often provided by viral regulatory elements. For example, commonly used promoters are derived from polyoma, Adenovirus 2, cytomegalovirus and Simian Virus 40. For other suitable expression systems for both prokaryotic and eukaryotic cells see chapters 16 and 17 of Sambrook, J., Fritsh, E. F., and Maniatis, T. Molecular Cloning: A Laboratory Manual. 2^(nd) , ed., Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1989.

[0104] In another embodiment, the recombinant mammalian expression vector is capable of directing expression of the nucleic acid preferentially in a particular cell type (e.g., tissue-specific regulatory elements are used to express the nucleic acid). Tissue-specific regulatory elements are known in the art. Non-limiting examples of suitable tissue-specific promoters include the albumin promoter (liver-specific; Pinkert et al. (1987) Genes Dev. 1:268-277), lymphoid-specific promoters (Calame and Eaton (1988) Adv. Immunol. 43:235-275), in particular promoters of T cell receptors (Winoto and Baltimore (1989) EMBO J. 8:729-733) and immunoglobulins (Banerji et al. (1983) Cell 33:729-740; Queen and Baltimore (1983) Cell 33:741-748), neuron-specific promoters (e.g., the neurofilament promoter; Byrne and Ruddle (1989) PNAS 86:5473-5477), pancreas-specific promoters (Edlund et al. (1985) Science 230:912-916), and mammary gland-specific promoters (e.g., milk whey promoter; U.S. Pat. No. 4,873,316 and European Application Publication No. 264,166). Developmentally-regulated promoters are also encompassed, for example the murine hox promoters (Kessel and Gruss (1990) Science 249:374-379) and the α-fetoprotein promoter (Campes and Tilghman (1989) Genes Dev. 3:537-546).

[0105] The invention further provides a recombinant expression vector comprising a DNA molecule of the invention cloned into the expression vector in an antisense orientation. That is, the DNA molecule is operatively linked to a regulatory sequence in a manner which allows for expression (by transcription of the DNA molecule) of an RNA molecule which is antisense to MP mRNA. Regulatory sequences operatively linked to a nucleic acid cloned in the antisense orientation can be chosen which direct the continuous expression of the antisense RNA molecule in a variety of cell types, for instance viral promoters and/or enhancers, or regulatory sequences can be chosen which direct constitutive, tissue specific or cell type specific expression of antisense RNA. The antisense expression vector can be in the form of a recombinant plasmid, phagemid or attenuated virus in which antisense nucleic acids are produced under the control of a high efficiency regulatory region, the activity of which can be determined by the cell type into which the vector is introduced. For a discussion of the regulation of gene expression using antisense genes see Weintraub, H. et al., Antisense RNA as a molecular tool for genetic analysis, Reviews—Trends in Genetics, Vol. 1(1) 1986.

[0106] Another aspect of the invention pertains to host cells into which a recombinant expression vector of the invention has been introduced. The terms “host cell” and “recombinant host cell” are used interchangeably herein. It is understood that such terms refer not only to the particular subject cell but to the progeny or potential progeny of such a cell. Because certain modifications may occur in succeeding generations due to either mutation or environmental influences, such progeny may not, in fact, be identical to the parent cell, but are still included within the scope of the term as used herein.

[0107] A host cell can be any prokaryotic or eukaryotic cell. For example, an MP protein can be expressed in bacterial cells such as C. glutamicum, insect cells, yeast or mammalian cells (such as Chinese hamster ovary cells (CHO) or COS cells). Other suitable host cells are known to those of ordinary skill in the art. Microorganisms related to Corynebacterium glutamicum which may be conveniently used as host cells for the nucleic acid and protein molecules of the invention are set forth in Table 3.

[0108] Vector DNA can be introduced into prokaryotic or eukaryotic cells via conventional transformation or transfection techniques. As used herein, the terms “transformation” and “transfection”, “conjugation” and “transduction” are intended to refer to a variety of art-recognized techniques for introducing foreign nucleic acid (e.g., linear DNA or RNA (e.g., a linearized vector or a gene construct alone without a vector) or nucleic acid in the form of a vector (e.g., a plasmid, phage, phasmid, phagemid, transposon or other DNA) into a host cell, including calcium phosphate or calcium chloride co-precipitation, DEAE-dextran-mediated transfection, lipofection, natural competence, chemical-mediated transfer, or electroporation. Suitable methods for transforming or transfecting host cells can be found in Sambrook, et al. (Molecular Cloning: A Laboratory Manual. 2^(nd) , ed., Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1989), and other laboratory manuals.

[0109] For stable transfection of mammalian cells, it is known that, depending upon the expression vector and transfection technique used, only a small fraction of cells may integrate the foreign DNA into their genome. In order to identify and select these integrants, a gene that encodes a selectable marker (e.g., resistance to antibiotics) is generally introduced into the host cells along with the gene of interest. Preferred selectable markers include those which confer resistance to drugs, such as G418, hygromycin and methotrexate. Nucleic acid encoding a selectable marker can be introduced into a host cell on the same vector as that encoding an MP protein or can be introduced on a separate vector. Cells stably transfected with the introduced nucleic acid can be identified by drug selection (e.g., cells that have incorporated the selectable marker gene will survive, while the other cells die).

[0110] To create a homologous recombinant microorganism, a vector is prepared which contains at least a portion of an MP gene into which a deletion, addition or substitution has been introduced to thereby alter, e.g., functionally disrupt, the MP gene. Preferably, this MP gene is a Corynebacterium glutamicum MP gene, but it can be a homologue from a related bacterium or even from a mammalian, yeast, or insect source. In a preferred embodiment, the vector is designed such that, upon homologous recombination, the endogenous MP gene is functionally disrupted (ie., no longer encodes a functional protein; also referred to as a “knock out” vector). Alternatively, the vector can be designed such that, upon homologous recombination, the endogenous MP gene is mutated or otherwise altered but still encodes functional protein (e.g., the upstream regulatory region can be altered to thereby alter the expression of the endogenous MP protein). In the homologous recombination vector, the altered portion of the MP gene is flanked at its 5′ and 3′ ends by additional nucleic acid of the MP gene to allow for homologous recombination to occur between the exogenous MP gene carried by the vector and an endogenous MP gene in a microorganism. The additional flanking MP nucleic acid is of sufficient length for successful homologous recombination with the endogenous gene. Typically, several kilobases of flanking DNA (both at the 5′ and 3′ ends) are included in the vector (see e.g., Thomas, K. R., and Capecchi, M. R. (1987) Cell 51: 503 for a description of homologous recombination vectors). The vector is introduced into a microorganism (e.g., by electroporation) and cells in which the introduced MP gene has homologously recombined with the endogenous MP gene are selected, using art-known techniques.

[0111] In another embodiment, recombinant microorganisms can be produced which contain selected systems which allow for regulated expression of the introduced gene. For example, inclusion of an MP gene on a vector placing it under control of the lac operon permits expression of the MP gene only in the presence of IPTG. Such regulatory systems are well known in the art.

[0112] In another embodiment, an endogenous MP gene in a host cell is disrupted (e.g., by homologous recombination or other genetic means known in the art) such that expression of its protein product does not occur. In another embodiment, an endogenous or introduced MP gene in a host cell has been altered by one or more point mutations, deletions, or inversions, but still encodes a functional MP protein. In still another embodiment, one or more of the regulatory regions (e.g., a promoter, repressor, or inducer) of an MP gene in a microorganism has been altered (e.g., by deletion, truncation, inversion, or point mutation) such that the expression of the MP gene is modulated. One of ordinary skill in the art will appreciate that host cells containing more than one of the described MP gene and protein modifications may be readily produced using the methods of the invention, and are meant to be included in the present invention.

[0113] A host cell of the invention, such as a prokaryotic or eukaryotic host cell in culture, can be used to produce (i. e., express) an MP protein. Accordingly, the invention further provides methods for producing MP proteins using the host cells of the invention. In one embodiment, the method comprises culturing the host cell of invention (into which a recombinant expression vector encoding an MP protein has been introduced, or into which genome has been introduced a gene encoding a wild-type or altered MP protein) in a suitable medium until MP protein is produced. In another embodiment, the method further comprises isolating MP proteins from the medium or the host cell.

[0114] C. Isolated MP Proteins

[0115] Another aspect of the invention pertains to isolated MP proteins, and biologically active portions thereof. An “isolated” or “purified” protein or biologically active portion thereof is substantially free of cellular material when produced by recombinant DNA techniques, or chemical precursors or other chemicals when chemically synthesized. The language “substantially free of cellular material” includes preparations of MP protein in which the protein is separated from cellular components of the cells in which it is naturally or recombinantly produced. In one embodiment, the language “substantially free of cellular material” includes preparations of MP protein having less than about 30% (by dry weight) of non-MP protein (also referred to herein as a “contaminating protein”), more preferably less than about 20% of non-MP protein, still more preferably less than about 10% of non-MP protein, and most preferably less than about 5% non-MP protein. When the MP protein or biologically active portion thereof is recombinantly produced, it is also preferably substantially free of culture medium, i.e., culture medium represents less than about 20%, more preferably less than about 10%, and most preferably less than about 5% of the volume of the protein preparation. The language “substantially free of chemical precursors or other chemicals” includes preparations of MP protein in which the protein is separated from chemical precursors or other chemicals which are involved in the synthesis of the protein. In one embodiment, the language “substantially free of chemical precursors or other chemicals” includes preparations of MP protein having less than about 30% (by dry weight) of chemical precursors or non-MP chemicals, more preferably less than about 20% chemical precursors or non-MP chemicals, still more preferably less than about 10% chemical precursors or non-MP chemicals, and most preferably less than about 5% chemical precursors or non-MP chemicals. In preferred embodiments, isolated proteins or biologically active portions thereof lack contaminating proteins from the same organism from which the MP protein is derived. Typically, such proteins are produced by recombinant expression of, for example, a C. glutamicum MP protein in a microorganism such as C. glutamicum.

[0116] An isolated MP protein or a portion thereof of the invention can catalyze an enzymatic reaction in an amino acid, vitamin, cofactor, nutraceutical, nucleotide, nucleoside, or trehalose metabolic pathway, or has one or more of the activities set forth in Table 1. In preferred embodiments, the protein or portion thereof comprises an amino acid sequence which is sufficiently homologous to an amino acid sequence of the invention (e.g., a sequence of an even-numbered SEQ ID NO: of the Sequence Listing) such that the protein or portion thereof maintains the ability to catalyze an enzymatic reaction in an amino acid, vitamin, cofactor, nutraceutical, nucleotide, nucleoside, or trehalose metabolic pathway. The portion of the protein is preferably a biologically active portion as described herein. In another preferred embodiment, an MP protein of the invention has an amino acid sequence set forth as an even-numbered SEQ ID NO: of the Sequence Listing. In yet another preferred embodiment, the MP protein has an amino acid sequence which is encoded by a nucleotide sequence which hybridizes, e.g., hybridizes under stringent conditions, to a nucleotide sequence of the invention (e.g., a sequence of an odd-numbered SEQ ID NO: of the Sequence Listing). In still another preferred embodiment, the MP protein has an amino acid sequence which is encoded by a nucleotide sequence that is at least about 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, or 60%, preferably at least about 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, or 70%, more preferably at least about 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, or 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, or 90%, or 91%, 92%, 93%, 94%, and even more preferably at least about 95%, 96%, 97%, 98%, 99%, 99.7% or more homologous to one of the nucleic acid sequences of the invention, or a portion thereof. Ranges and identity values intermediate to the above-recited values, (e.g., 70-90% identical or 80-95% identical) are also intended to be encompassed by the present invention. For example, ranges of identity values using a combination of any of the above values recited as upper and/or lower limits are intended to be included. The preferred MP proteins of the present invention also preferably possess at least one of the MP activities described herein. For example, a preferred MP protein of the present invention includes an amino acid sequence encoded by a nucleotide sequence which hybridizes, e.g., hybridizes under stringent conditions, to a nucleotide sequence of the invention, and which can catalyze an enzymatic reaction in an amino acid, vitamin, cofactor, nutraceutical, nucleotide, nucleoside, or trehalose metabolic pathway, or which has one or more of the activities set forth in Table 1.

[0117] In other embodiments, the MP protein is substantially homologous to an amino acid sequence of the invention (e.g., a sequence of an even-numbered SEQ ID NO: of the Sequence Listing) and retains the functional activity of the protein of one of the amino acid sequences of the invention yet differs in amino acid sequence due to natural variation or mutagenesis, as described in detail in subsection I above. Accordingly, in another embodiment, the MP protein is a protein which comprises an amino acid sequence which is at least about 50%, 51%, 52%, 53%, 54%, 55%, 56%, 57%, 58%, 59%, or 60%, preferably at least about 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, or 70%, more preferably at least about 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, or 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, or 90%, or 91%, 92%, 93%, 94%, and even more preferably at least about 95%, 96%, 97%, 98%, 99%, 99.7% or more homologous to an entire amino acid sequence of the invention and which has at least one of the MP activities described herein. Ranges and identity values intermediate to the above-recited values, (e.g., 70-90% identical or 80-95% identical) are also intended to be encompassed by the present invention. For example, ranges of identity values using a combination of any of the above values recited as upper and/or lower limits are intended to be included. In another embodiment, the invention pertains to a full length C. glutamicum protein which is substantially homologous to an entire amino acid sequence of the invention.

[0118] Biologically active portions of an MP protein include peptides comprising amino acid sequences derived from the amino acid sequence of an MP protein, e.g., an amino acid sequence of an even-numbered SEQ ID NO: of the Sequence Listing or the amino acid sequence of a protein homologous to an MP protein, which include fewer amino acids than a full length MP protein or the full length protein which is homologous to an MP protein, and exhibit at least one activity of an MP protein. Typically, biologically active portions (peptides, e.g., peptides which are, for example, 5, 10, 15, 20, 30, 35, 36, 37, 38, 39, 40, 50, 100 or more amino acids in length) comprise a domain or motif with at least one activity of an MP protein. Moreover, other biologically active portions, in which other regions of the protein are deleted, can be prepared by recombinant techniques and evaluated for one or more of the activities described herein. Preferably, the biologically active portions of an MP protein include one or more selected domains/motifs or portions thereof having biological activity.

[0119] MP proteins are preferably produced by recombinant DNA techniques. For example, a nucleic acid molecule encoding the protein is cloned into an expression vector (as described above), the expression vector is introduced into a host cell (as described above) and the MP protein is expressed in the host cell. The MP protein can then be isolated from the cells by an appropriate purification scheme using standard protein purification techniques. Alternative to recombinant expression, an MP protein, polypeptide, or peptide can be synthesized chemically using standard peptide synthesis techniques. Moreover, native MP protein can be isolated from cells (e.g., endothelial cells), for example using an anti-MP antibody, which can be produced by standard techniques utilizing an MP protein or fragment thereof of this invention.

[0120] The invention also provides MP chimeric or fusion proteins. As used herein, an MP “chimeric protein” or “fusion protein” comprises an MP polypeptide operatively linked to a non-MP polypeptide. An “MP polypeptide” refers to a polypeptide having an amino acid sequence corresponding to MP, whereas a “non-MP polypeptide” refers to a polypeptide having an amino acid sequence corresponding to a protein which is not substantially homologous to the MP protein, e.g., a protein which is different from the MP protein and which is derived from the same or a different organism. Within the fusion protein, the term “operatively linked” is intended to indicate that the MP polypeptide and the non-MP polypeptide are fused in-frame to each other. The non-MP polypeptide can be fused to the N-terminus or C-terminus of the MP polypeptide. For example, in one embodiment the fusion protein is a GST-MP fusion protein in which the MP sequences are fused to the C-terminus of the GST sequences. Such fusion proteins can facilitate the purification of recombinant MP proteins. In another embodiment, the fusion protein is an MP protein containing a heterologous signal sequence at its N-terminus. In certain host cells (e.g., mammalian host cells), expression and/or secretion of an MP protein can be increased through use of a heterologous signal sequence.

[0121] Preferably, an MP chimeric or fusion protein of the invention is produced by standard recombinant DNA techniques. For example, DNA fragments coding for the different polypeptide sequences are ligated together in-frame in accordance with conventional techniques, for example by employing blunt-ended or stagger-ended termini for ligation, restriction enzyme digestion to provide for appropriate termini, filling-in of cohesive ends as appropriate, alkaline phosphatase treatment to avoid undesirable joining, and enzymatic ligation. In another embodiment, the fusion gene can be synthesized by conventional techniques including automated DNA synthesizers. Alternatively, PCR amplification of gene fragments can be carried out using anchor primers which give rise to complementary overhangs between two consecutive gene fragments which can subsequently be annealed and reamplified to generate a chimeric gene sequence (see, for example, Current Protocols in Molecular Biology, eds. Ausubel et al. John Wiley & Sons: 1992). Moreover, many expression vectors are commercially available that already encode a fusion moiety (e.g., a GST polypeptide). An MP-encoding nucleic acid can be cloned into such an expression vector such that the fusion moiety is linked in-frame to the MP protein.

[0122] Homologues of the MP protein can be generated by mutagenesis, e.g., discrete point mutation or truncation of the MP protein. As used herein, the term “homologue” refers to a variant form of the MP protein which acts as an agonist or antagonist of the activity of the MP protein. An agonist of the MP protein can retain substantially the same, or a subset, of the biological activities of the MP protein. An antagonist of the MP protein can inhibit one or more of the activities of the naturally occurring form of the MP protein, by, for example, competitively binding to a downstream or upstream member of the MP cascade which includes the MP protein. Thus, the C. glutamicum MP protein and homologues thereof of the present invention may modulate the activity of one or more metabolic pathways in which MP proteins play a role in this microorganism.

[0123] In an alternative embodiment, homologues of the MP protein can be identified by screening combinatorial libraries of mutants, e.g., truncation mutants, of the MP protein for MP protein agonist or antagonist activity. In one embodiment, a variegated library of MP variants is generated by combinatorial mutagenesis at the nucleic acid level and is encoded by a variegated gene library. A variegated library of MP variants can be produced by, for example, enzymatically ligating a mixture of synthetic oligonucleotides into gene sequences such that a degenerate set of potential MP sequences is expressible as individual polypeptides, or alternatively, as a set of larger fusion proteins (e.g., for phage display) containing the set of MP sequences therein. There are a variety of methods which can be used to produce libraries of potential MP homologues from a degenerate oligonucleotide sequence. Chemical synthesis of a degenerate gene sequence can be performed in an automatic DNA synthesizer, and the synthetic gene then ligated into an appropriate expression vector. Use of a degenerate set of genes allows for the provision, in one mixture, of all of the sequences encoding the desired set of potential MP sequences. Methods for synthesizing degenerate oligonucleotides are known in the art (see, e.g., Narang, S. A. (1983) Tetrahedron 39:3; Itakura et al. (1984) Annu. Rev. Biochem. 53:323; Itakura et al. (1984) Science 198:1056; Ike et al. (1983) Nucleic Acid Res. 11:477.

[0124] In addition, libraries of fragments of the MP protein coding can be used to generate a variegated population of MP fragments for screening and subsequent selection of homologues of an MP protein. In one embodiment, a library of coding sequence fragments can be generated by treating a double stranded PCR fragment of an MP coding sequence with a nuclease under conditions wherein nicking occurs only about once per molecule, denaturing the double stranded DNA, renaturing the DNA to form double stranded DNA which can include sense/antisense pairs from different nicked products, removing single stranded portions from reformed duplexes by treatment with S1 nuclease, and ligating the resulting fragment library into an expression vector. By this method, an expression library can be derived which encodes N-terminal, C-terminal and internal fragments of various sizes of the MP protein.

[0125] Several techniques are known in the art for screening gene products of combinatorial libraries made by point mutations or truncation, and for screening cDNA libraries for gene products having a selected property. Such techniques are adaptable for rapid screening of the gene libraries generated by the combinatorial mutagenesis of MP homologues. The most widely used techniques, which are amenable to high through-put analysis, for screening large gene libraries typically include cloning the gene library into replicable expression vectors, transforming appropriate cells with the resulting library of vectors, and expressing the combinatorial genes under conditions in which detection of a desired activity facilitates isolation of the vector encoding the gene whose product was detected. Recursive ensemble mutagenesis (REM), a new technique which enhances the frequency of functional mutants in the libraries, can be used in combination with the screening assays to identify MP homologues (Arkin and Yourvan (1992) PNAS 89:7811-7815; Delgrave et al. (1993) Protein Engineering 6(3):327-331).

[0126] In another embodiment, cell based assays can be exploited to analyze a variegated MP library, using methods well known in the art.

[0127] D. Uses and Methods of the Invention

[0128] The nucleic acid molecules, proteins, protein homologues, fusion proteins, primers, vectors, and host cells described herein can be used in one or more of the following methods: identification of C. glutamicum and related organisms; mapping of genomes of organisms related to C. glutamicum; identification and localization of C. glutamicum sequences of interest; evolutionary studies; determination of MP protein regions required for function; modulation of an MP protein activity; modulation of the activity of an MP pathway; and modulation of cellular production of a desired compound, such as a fine chemical.

[0129] The MP nucleic acid molecules of the invention have a variety of uses. First, they may be used to identify an organism as being Corynebacterium glutamicum or a close relative thereof. Also, they may be used to identify the presence of C. glutamicum or a relative thereof in a mixed population of microorganisms. The invention provides the nucleic acid sequences of a number of C. glutamicum genes; by probing the extracted genomic DNA of a culture of a unique or mixed population of microorganisms under stringent conditions with a probe spanning a region of a C. glutamicum gene which is unique to this organism, one can ascertain whether this organism is present. Although Corynebacterium glutamicum itself is not pathogenic to humans, it is related to species which are human pathogens, such as Corynebacterium diphtheriae. Corynebacterium diphtheriae is the causative agent of diphtheria, a rapidly developing, acute, febrile infection which involves both local and systemic pathology. In this disease, a local lesion develops in the upper respiratory tract and involves necrotic injury to epithelial cells; the bacilli secrete toxin which is disseminated through this lesion to distal susceptible tissues of the body. Degenerative changes brought about by the inhibition of protein synthesis in these tissues, which include heart, muscle, peripheral nerves, adrenals, kidneys, liver and spleen, result in the systemic pathology of the disease. Diphtheria continues to have high incidence in many parts of the world, including Africa, Asia, Eastern Europe and the independent states of the former Soviet Union. An ongoing epidemic of diphtheria in the latter two regions has resulted in at least 5,000 deaths since 1990.

[0130] In one embodiment, the invention provides a method of identifying the presence or activity of Cornyebacterium diphtheriae in a subject. This method includes detection of one or more of the nucleic acid or amino acid sequences of the invention (e.g., the sequences set forth as odd-numbered or even-numbered SEQ ID NOs, respectively, in the Sequence Listing) in a subject, thereby detecting the presence or activity of Corynebacterium diphtheriae in the subject. C. glutamicum and C. diphtheriae are related bacteria, and many of the nucleic acid and protein molecules in C. glutamicum are homologous to C. diphtheriae nucleic acid and protein molecules, and can therefore be used to detect C. diphtheriae in a subject.

[0131] The nucleic acid and protein molecules of the invention may also serve as markers for specific regions of the genome. This has utility not only in the mapping of the genome, but also for functional studies of C. glutamicum proteins. For example, to identify the region of the genome to which a particular C. glutamicum DNA-binding protein binds, the C. glutamicum genome could be digested, and the fragments incubated with the DNA-binding protein. Those which bind the protein may be additionally probed with the nucleic acid molecules of the invention, preferably with readily detectable labels; binding of such a nucleic acid molecule to the genome fragment enables the localization of the fragment to the genome map of C. glutamicum, and, when performed multiple times with different enzymes, facilitates a rapid determination of the nucleic acid sequence to which the protein binds. Further, the nucleic acid molecules of the invention may be sufficiently homologous to the sequences of related species such that these nucleic acid molecules may serve as markers for the construction of a genomic map in related bacteria, such as Brevibacterium lactofermentum.

[0132] The MP nucleic acid molecules of the invention are also useful for evolutionary and protein structural studies. The metabolic processes in which the molecules of the invention participate are utilized by a wide variety of prokaryotic and eukaryotic cells; by comparing the sequences of the nucleic acid molecules of the present invention to those encoding similar enzymes from other organisms, the evolutionary relatedness of the organisms can be assessed. Similarly, such a comparison permits an assessment of which regions of the sequence are conserved and which are not, which may aid in determining those regions of the protein which are essential for the functioning of the enzyme. This type of determination is of value for protein engineering studies and may give an indication of what the protein can tolerate in terms of mutagenesis without losing function.

[0133] Manipulation of the MP nucleic acid molecules of the invention may result in the production of MP proteins having functional differences from the wild-type MP proteins. These proteins may be improved in efficiency or activity, may be present in greater numbers in the cell than is usual, or may be decreased in efficiency or activity.

[0134] The invention also provides methods for screening molecules which modulate the activity of an MP protein, either by interacting with the protein itself or a substrate or binding partner of the MP protein, or by modulating the transcription or translation of an MP nucleic acid molecule of the invention. In such methods, a microorganism expressing one or more MP proteins of the invention is contacted with one or more test compounds, and the effect of each test compound on the activity or level of expression of the MP protein is assessed.

[0135] When the desired fine chemical to be isolated from large-scale fermentative culture of C. glutamicum is an amino acid, a vitamin, a cofactor, a nutraceutical, a nucleotide, a nucleoside, or trehalose, modulation of the activity or efficiency of activity of one or more of the proteins of the invention by recombinant genetic mechanisms may directly impact the production of one of these fine chemicals. For example, in the case of an enzyme in a biosynthetic pathway for a desired amino acid, improvement in efficiency or activity of the enzyme (including the presence of multiple copies of the gene) should lead to an increased production or efficiency of production of that desired amino acid. In the case of an enzyme in a biosynthetic pathway for an amino acid whose synthesis is in competition with the synthesis of a desired amino acid, any decrease in the efficiency or activity of this enzyme (including deletion of the gene) should result in an increase in production or efficiency of production of the desired amino acid, due to decreased competition for intermediate compounds and/or energy. In the case of an enzyme in a degradation pathway for a desired amino acid, any decrease in efficiency or activity of the enzyme should result in a greater yield or efficiency of production of the desired product due to a decrease in its degradation. Lastly, mutagenesis of an enzyme involved in the biosynthesis of a desired amino acid such that this enzyme is no longer is capable of feedback inhibition should result in increased yields or efficiency of production of the desired amino acid. The same should apply to the biosynthetic and degradative enzymes of the invention involved in the metabolism of vitamins, cofactors, nutraceuticals, nucleotides, nucleosides and trehalose.

[0136] Similarly, when the desired fine chemical is not one of the aforementioned compounds, the modulation of activity of one of the proteins of the invention may still impact the yield and/or efficiency of production of the compound from large-scale culture of C. glutamicum. The metabolic pathways of any organism are closely interconnected; the intermediate used by one pathway is often supplied by a different pathway. Enzyme expression and function may be regulated based on the cellular levels of a compound from a different metabolic process, and the cellular levels of molecules necessary for basic growth, such as amino acids and nucleotides, may critically affect the viability of the microorganism in large-scale culture. Thus, modulation of an amino acid biosynthesis enzyme, for example, such that it is no longer responsive to feedback inhibition or such that it is improved in efficiency or turnover may result in increased cellular levels of one or more amino acids. In turn, this increased pool of amino acids provides not only an increased supply of molecules necessary for protein synthesis, but also of molecules which are utilized as intermediates and precursors in a number of other biosynthetic pathways. If a particular amino acid had been limiting in the cell, its increased production might increase the ability of the cell to perform numerous other metabolic reactions, as well as enabling the cell to more efficiently produce proteins of all kinds, possibly increasing the overall growth rate or survival ability of the cell in large scale culture. Increased viability improves the number of cells capable of producing the desired fine chemical in fermentative culture, thereby increasing the yield of this compound. Similar processes are possible by the modulation of activity of a degradative enzyme of the invention such that the enzyme no longer catalyzes, or catalyzes less efficiently, the degradation of a cellular compound which is important for the biosynthesis of a desired compound, or which will enable the cell to grow and reproduce more efficiently in large-scale culture. It should be emphasized that optimizing the degradative activity or decreasing the biosynthetic activity of certain molecules of the invention may also have a beneficial effect on the production of certain fine chemicals from C. glutamicum. For example, by decreasing the efficiency of activity of a biosynthetic enzyme in a pathway which competes with the biosynthetic pathway of a desired compound for one or more intermediates, more of those intermediates should be available for conversion to the desired product. A similar situation may call for the improvement of degradative ability or efficiency of one or more proteins of the invention.

[0137] This aforementioned list of mutagenesis strategies for MP proteins to result in increased yields of a desired compound is not meant to be limiting; variations on these mutagenesis strategies will be readily apparent to one of ordinary skill in the art. By these mechanisms, the nucleic acid and protein molecules of the invention may be utilized to generate C. glutamicum or related strains of bacteria expressing mutated MP nucleic acid and protein molecules such that the yield, production, and/or efficiency of production of a desired compound is improved. This desired compound may be any natural product of C. glutamicum, which includes the final products of biosynthesis pathways and intermediates of naturally-occurring metabolic pathways, as well as molecules which do not naturally occur in the metabolism of C. glutamicum, but which are produced by a C. glutamicum strain of the invention. Preferred compounds to be produced by Corynebacterium glutamicum strains are the amino acids L-lysine and L-methionine.

[0138] In one embodiment, the metC gene encoding cystathionine β-lyase, the third enzyme in the methionine biosynthetic pathway, was isolated from Corynebacterium glutamicum. The translational product of the gene showed no significant homology with that of metC gene from other organisms. Introduction of the plasmid containing the metC gene into C. glutamicum resulted in a 5-fold increase in the activity of cystathionine β-lyase. The protein product, now designated MetC (corresponding to SEQ ID NO:4), which encodes a protein product of 35,574 Daltons and consists of 325 amino acids, is identical to the previously reported aecD gene (Rossol, I. and Puhler, A. (1992) J. Bacteriology 174, 2968-2977) except the existence of two different amino acids. Like aecD gene, when present in multiple copies, metC gene conferred resistance to S-(β-aminoethyl)-cysteine which is a toxic lysine analog. However, genetic and biochemical evidences suggest that the natural activity of metC gene product is to mediate methionine biosynthesis in C. glutamicum. Mutant strains of metC were constructed and the strains showed methionine prototrophy. The mutant strains completely lost their ability to show resistance to S-(γ-aminoethyl)-cysteine. These results show that, in addition to the transsulfuration, which is another biosynthetic pathway, the direct sulfhydrylation pathway is functional in C. glutamicum as a parallel biosynthetic route for methionine.

[0139] In yet another embodiment, it is also shown that the additional sulfhydrylation pathway is catalyzed by O-acetylhomoserine sulfhydrylase. The presence of the pathway is demonstrated by the isolation of the corresponding metZ (or metY) gene and enzyme (corresponding to SEQ ID NO: 1 and SEQ ID NO:2, respectively). Among the eukaryotes, fungi and yeast species have been reported to have both the transsulfuration and direct sulfhydrylation pathway. Thus far, no prokaryotic organism which possesses both pathways has been found. Unlike E. coli which only possesses single biosynthetic route for lysine, C. glutamicum possesses two parallel biosynthetic pathways for the amino acid. The biosynthetic pathway for methionine in C. glutamicum is analogous to that of lysine in that aspect.

[0140] The gene metZ is located in the upstream region of metA, which is the gene encoding the enzyme catalysing the first step of methionine biosynthesis (Park, S.-D., et al. (1998) Mol. Cells 8, 286-294). Regions upstream and downstream of metA were sequenced to identify other met genes. It appears that metZ and metA form an operon. Expression of the genes encoding MetA and MetZ leads to overproduction of the corresponding polypeptides.

[0141] Surprisingly, metZ clones can complement methionine auxotrophic Escherichia coli metB mutant strains. This shows that the protein product of metZ catalyzes a step that can bypass the step catalyzed by the protein product of metB. MetZ was also disrupted and the mutant strain showed methionine prototrophy. Corynebacterium glutamicum metB and metZ double mutants were also constructed. The double mutant is auxotrophic for methionine. Thus, metZ encodes a protein catalysing the reaction from O-Acetyl-Homoserine to Homo cysteine, which is one step in the sulfhydrylation pathway of methionine biosynthesis. Corynebacterium glutamicum contains both the transsulfuration and the sulfhydrylation pathway of methionine biosynthesis.

[0142] Introduction of metZ into C. glutamicum resulted in the expression of a 47,000 Dalton protein. Combined introduction of metZ and metA in C. glutamicum resulted in the appearance of metA and metZ proteins as shown by gel electrophoresis. If the Corynebacterium strain is a lysine overproducer, introduction of a plasmid containing metZ and metA resulted in a lower lysine titer but accumulation of homocysteine and methionine is detected.

[0143] In another embodiment metZ and metA were introduced into Corynebacterium glutamicum strains together with the horn gene, encoding the homoserine dehydrogenase, catalysing the conversion from aspartate semialdehyde to homoserine. Different hom genes from different organisms were chosen for this experiment. The Corynebacterium glutamicum hom gene can be used as well as hom genes from other procaryotes like Escherichia coli or Bacillus subtilis or the hom gene of eukaryotes such as Saccharomyces cerevisiae, Shizosaccharomyces pombe, Ashbya gossypii or algae, higher plants or animals. It may be that the hom gene is insensitive against feed back inhibition mediated by any metabolites that occur in the biosynthetic routes of the amino acids of the aspartate family, like aspatrate, lysine, threonine or methionine. Such metabolites are for example aspartate, lysine, methionine, threonine, aspartyl-phosphate, aspartate semialdehyd, homoserine, cystathionine, homocysteine or any other metabolite that occurs in this biosynthetic routes. In addition to the metabolites, the homoserine dehydrogenase may be insensitive against inhibition by analogues of all those metabolites or even against other compounds involved in this metabolism as there are other amino acids like cysteine or cofactors like vitamin B12 and all of its derivatives and S-adenosylmethionine and its metabolites and derivatives and analogues. The insensitivity of the homoserine dehydrogenase against all these, a part of these or only one of these compounds may either be its natural attitude or it may be the result from one or more mutations that resulted from classical mutation and selection using chemicals or irradiation or other mutagens. The mutations could also be introduced into the hom gene using gene technology, for example the introduction of site specific point mutations or by any method aforementioned for the MP or MP encoding DNA-sequences.

[0144] When a hom gene was combined with the metZ and metA genes and introduced into a Corynebacterium glutamicum strain that is a lysine overproducer, lysine accumulation was reduced and homocysteine and methionine accumulation was enhanced. A further enhancement of homocysteine and methionine concentrations can be achieved, if a lysine overproducing Corynebacterium glutamicum strain is used and a disruption of the ddh gene or the lysA gene was introduced prior to the transformation with DNA containing a hom gene and metZ and metA in combination. The overproduction of homocysteine and methionine was possible using different sulfur sources. Sulfates, thiosulfates, sulfites and also more reduced sulfur sources like H₂S and sulfides and derivatives could be used. Also, organic sulfur sources like methyl mercaptan, thioglycolates, thiocyanates, thiourea, sulfur containing amino acids like cysteine and other sulfur containing compounds can be used to achieve homocysteine and methionine overproduction.

[0145] In another embodiment, the metC gene was introduced into a Corynebacterium glutamicum strain using aforementioned methods. The metC gene can be transformed into the strain in combination with other genes like metB, meta and metA. The hom gene can also be added. When the hom gene, the met C, metA and metB genes were combined on a vector and introduced into a Corynebacterium glutamicurm strain, homocysteine and methionine overproduction was achieved. The overproduction of homocysteine and methionine was possible using different sulfur sources. Sulfates, thiosulfates, sulfites and also more reduced sulfur sources like H₂S and sulfides and derivatives could be used. Also, organic sulfur sources like methyl mercaptan, thioglycolates, thiocyanates, thiourea, sulfur containing amino acids like cysteine and other sulfur containing compounds can be used to achieve homocysteine and methionine overproduction.

[0146] This invention is further illustrated by the following examples which should not be construed as limiting. The contents of all references, patent applications, patents, published patent applications, Tables, and the sequence listing cited throughout this application are hereby incorporated by reference.

[0147] Exemplification

EXAMPLE 1

[0148] Preparation of Total Genomic DNA of Corynebacterium glutamicum ATCC13032

[0149] A culture of Corynebacterium glutamicum (ATCC 13032) was grown overnight at 30° C. with vigorous shaking in BHI medium (Difco). The cells were harvested by centrifugation, the supernatant was discarded and the cells were resuspended in 5 ml buffer-I (5% of the original volume of the culture—all indicated volumes have been calculated for 100 ml of culture volume). Composition of buffer-I: 140.34 g/l sucrose, 2.46 g/l MgSO₄×7H₂O, 10 ml/l KH₂PO₄ solution (100 g/l, adjusted to pH 6.7 with KOH), 50 ml/l M12 concentrate (10 g/l (NH₄)₂SO₄, 1 g/l NaCl, 2 g/l MgSO₄×7H₂O, 0.2 g/l CaCl₂, 0.5 g/l yeast extract (Difco), 10 ml/l trace-elements-mix (200 mg/l FeSO₄×H₂O, 10 mg/l ZnSO₄×7 H₂O, 3 mg/l MnCl₂×4 H₂O, 30 mg/l H₃BO₃ 20 mg/l CoCl₂×6 H₂O, 1 mg/l NiCl₂×6 H₂O, 3 mg/l Na₂MoO₄×2 H₂O, 500 mg/l complexing a (EDTA or critic acid), 100 ml/l vitamins-mix (0.2 mg/l biotin, 0.2 mg/l folic acid, 20 mg/l p-amino benzoic acid, 20 mg/l riboflavin, 40 mg/l ca-panthothenate, 140 mg/l nicotinic acid, 40 mg/l pyridoxole hydrochloride, 200 mg/l myo-inositol). Lysozyme was added to the suspension to a final concentration of 2.5 mg/ml. After an approximately 4 h incubation at 37° C., the cell wall was degraded and the resulting protoplasts are harvested by centrifugation. The pellet was washed once with 5 ml buffer-I and once with 5 ml TE-buffer (10 mM Tris-HCl, 1 mM EDTA, pH 8). The pellet was resuspended in 4 ml TE-buffer and 0.5 ml SDS solution (10%) and 0.5 ml NaCl solution (5 M) are added. After adding of proteinase K to a final concentration of 200 μg/ml, the suspension is incubated for ca. 18 h at 37° C. The DNA was purified by extraction with phenol, phenol-chloroform-isoamylalcohol and chloroform-isoamylalcohol using standard procedures. Then, the DNA was precipitated by adding {fraction (1/50)} volume of 3 M sodium acetate and 2 volumes of ethanol, followed by a 30 min incubation at −20° C. and a 30 min centrifugation at 12,000 rpm in a high speed centrifuge using a SS34 rotor (Sorvall). The DNA was dissolved in 1 ml TE-buffer containing 20 μg/ml RNaseA and dialysed at 4° C. against 1000 ml TE-buffer for at least 3 hours. During this time, the buffer was exchanged 3 times. To aliquots of 0.4 ml of the dialysed DNA solution, 0.4 ml of 2 M LiCl and 0.8 ml of ethanol are added. After a 30 min incubation at −20° C., the DNA was collected by centrifugation (13,000 rpm, Biofuge Fresco, Heraeus, Hanau, Germany). The DNA pellet was dissolved in TE-buffer. DNA prepared by this procedure could be used for all purposes, including southern blotting or construction of genomic libraries.

EXAMPLE 2

[0150] Construction of Genomic Libraries in Escherichia coli of Corynebacterium Glutamicum ATCC13032.

[0151] Using DNA prepared as described in Example 1, cosmid and plasmid libraries were constructed according to known and well established methods (see e.g., Sambrook, J. et al. (1989) “Molecular Cloning: A Laboratory Manual”, Cold Spring Harbor Laboratory Press, or Ausubel, F. M. et al. (1994) “Current Protocols in Molecular Biology”, John Wiley & Sons.)

[0152] Any plasmid or cosmid could be used. Of particular use were the plasmids pBR322 (Sutcliffe, J. G. (1979) Proc. Natl. Acad. Sci. USA, 75:3737-3741); pACYC177 (Change & Cohen (1978) J. Bacteriol 134:1141-1156), plasmids of the pBS series (pBSSK+, pBSSK− and others; Stratagene, LaJolla, USA), or cosmids as SuperCosl (Stratagene, LaJolla, USA) or Lorist6 (Gibson, T. J., Rosenthal A. and Waterson, R. H. (1987) Gene 53:283-286. Gene libraries specifically for use in C. glutamicum may be constructed using plasmid pSL109 (Lee, H.-S. and A. J. Sinskey (1994) J. Microbiol. Biotechnol. 4: 256-263).

[0153] For the isolation of metC clones, E. coli JE6839 cells were transformed with the library DNA and plated onto the M9 minimal medium containing ampicillin and appropriate supplements. The plates were incubated at 37° C. for 5 days. Colonies were isolated and screened for the plasmid content. The complete nucleotide sequence of the isolated metC gene was determined by methods well-known to one of ordinary skill in the art.

EXAMPLE 3

[0154] DNA Sequencing and Computational Functional Analysis

[0155] Genomic libraries as described in Example 2 were used for DNA sequencing according to standard methods, in particular by the chain termination method using ABI377 sequencing machines (see e.g., Fleischman, R. D. et al. (1995) “Whole-genome Random Sequencing and Assembly of Haemophilus Influenzae Rd., Science, 269:496-512). Sequencing primers with the following nucleotide sequences were used: 5′-GGAAACAGTATGACCATG-3′ (SEQ ID NO:123) or 5′-GTAAAACGACGGCCAGT-3′ (SEQ ID NO.: 124).

EXAMPLE 4

[0156] In vivo Mutagenesis

[0157] In vivo mutagenesis of Corynebacterium glutamicum can be performed by passage of plasmid (or other vector) DNA through E. coli or other microorganisms (e.g Bacillus spp. or yeasts such as Saccharomyces cerevisiae) which are impaired in their capabilities to maintain the integrity of their genetic information. Typical mutator strains have mutations in the genes for the DNA repair system (e.g., mutHLS, mutD, mutT, etc.; for reference, see Rupp, W. D. (1996) DNA repair mechanisms, in: Escherichia coli and Salmonella, p. 2277-2294, ASM: Washington.) Such strains are well known to those of ordinary skill in the art. The use of such strains is illustrated, for example, in Greener, A. and Callahan, M. (1994) Strategies 7: 32-34.

EXAMPLE 5

[0158] DNA Transfer Between Escherichia coli and Corynebacterium glutamicum

[0159] Several Corynebacterium and Brevibacterium species contain endogenous plasmids (as e.g., pHM1519 or pBL1) which replicate autonomously (for review see, e.g., Martin, J. F. et al. (1987) Biotechnology, 5:137-146). Shuttle vectors for Escherichia coil and Corynebacterium glutamicum can be readily constructed by using standard vectors for E. coli (Sambrook, J. et al. (1989), “Molecular Cloning: A Laboratory Manual”, Cold Spring Harbor Laboratory Press or Ausubel, F. M. et al. (1994) “Current Protocols in Molecular Biology”, John Wiley & Sons) to which a origin or replication for and a suitable marker from Corynebacterium glutamicum is added. Such origins of replication are preferably taken from endogenous plasmids isolated from Corynebacterium and Brevibacterium species. Of particular use as transformation markers for these species are genes for kanamycin resistance (such as those derived from the Tn5 or Tn903 transposons) or chloramphenicol (Winnacker, E. L. (1987) “From Genes to Clones—Introduction to Gene Technology, VCH, Weinheim). There are numerous examples in the literature of the construction of a wide variety of shuttle vectors which replicate in both E. coli and C. glutamicum, and which can be used for several purposes, including gene over-expression (for reference, see e.g., Yoshihama, M. et al (1985) J. Bacteriol. 162:591-597, Martin J. F. et al. (1987) Biotechnology, 5:137-146 and Eikmanns, B. J. et al. (1991) Gene, 102:93-98).

[0160] Using standard methods, it is possible to clone a gene of interest into one of the shuttle vectors described above and to introduce such a hybrid vectors into strains of Corynebacterium glutamicum. Transformation of C. glutamicum can be achieved by protoplast transformation (Kastsumata, R. et al. (1984) J. Bacteriol. 159306-311), electroporation (Liebl, E. et al. (1989) FEMS Microbiol. Letters, 53:399-303) and in cases where special vectors are used, also by conjugation (as described e.g. in Schäfer, A et al. (1990) J. Bacteriol. 172:1663-1666). It is also possible to transfer the shuttle vectors for C. glutamicum to E. coil by preparing plasmid DNA from C. glutamicum (using standard methods well-known in the art) and transforming it into E. coli. This transformation step can be performed using standard methods, but it is advantageous to use an Mcr-deficient E. coli strain, such as NM522 (Gough & Murray (1983) J. Mol. Biol. 166:1-19).

[0161] Genes may be overexpressed in C. glutamicum strains using plasmids which comprise pCG1 (U.S. Pat. No. 4,617,267) or fragments thereof, and optionally the gene for kanamycin resistance from TN903 (Grindley, N. D. and Joyce, C. M. (1980) Proc. Natl. Acad. Sci. USA 77(12): 7176-7180). In addition, genes may be overexpressed in C. glutamicum strains using plasmid pSL109 (Lee, H.-S. and A. J. Sinskey (1994) J. Microbiol Biotechnol. 4: 256-263).

[0162] Aside from the use of replicative plasmids, gene overexpression can also be achieved by integration into the genome. Genomic integration in C. glutamicum or other Corynebacterium or Brevibacterium species may be accomplished by well-known methods, such as homologous recombination with genomic region(s), restriction endonuclease mediated integration (REMI) (see, e.g., DE U.S. Pat. No. 19823834), or through the use of transposons. It is also possible to modulate the activity of a gene of interest by modifying the regulatory regions (e.g., a promoter, a repressor, and/or an enhancer) by sequence modification, insertion, or deletion using site-directed methods (such as homologous recombination) or methods based on random events (such as transposon mutagenesis or REMI). Nucleic acid sequences which function as transcriptional terminators may also be inserted 3′ to the coding region of one or more genes of the invention; such terminators are well-known in the art and are described, for example, in Winnacker, E. L. (1987) From Genes to Clones—Introduction to Gene Technology. VCH: Weinheim.

EXAMPLE 6

[0163] Assessment of the Expression of the Mutant Protein

[0164] Observations of the activity of a mutated protein in a transformed host cell rely on the fact that the mutant protein is expressed in a similar fashion and in a similar quantity to that of the wild-type protein. A useful method to ascertain the level of transcription of the mutant gene (an indicator of the amount of mRNA available for translation to the gene product) is to perform a Northern blot (for reference see, for example, Ausubel et al. (1988) Current Protocols in Molecular Biology, Wiley: New York), in which a primer designed to bind to the gene of interest is labeled with a detectable tag (usually radioactive or chemiluminescent), such that when the total RNA of a culture of the organism is extracted, run on gel, transferred to a stable matrix and incubated with this probe, the binding and quantity of binding of the probe indicates the presence and also the quantity of mRNA for this gene. This information is evidence of the degree of transcription of the mutant gene. Total cellular RNA can be prepared from Corynebacterium glutamicum by several methods, all well-known in the art, such as that described in Bormann, E. R. et al. (1992) Mol. Microbiol. 6: 317-326.

[0165] To assess the presence or relative quantity of protein translated from this mRNA, standard techniques, such as SDS-acrylamide gel electrophoresis, were employed. The overproduction of metC and metZ in combination with metA in Corynebacterium glutamicum was demonstrated by this method. Western blot may also be employed (see, for example, Ausubel et al. (1988) Current Protocols in Molecular Biology, Wiley: New York). In this process, total cellular proteins are extracted, separated by gel electrophoresis, transferred to a matrix such as nitrocellulose, and incubated with a probe, such as an antibody, which specifically binds to the desired protein. This probe is generally tagged with a chemiluminescent or calorimetric label which may be readily detected. The presence and quantity of label observed indicates the presence and quantity of the desired mutant protein present in the cell.

EXAMPLE 7

[0166] Growth of Escherichia coli and Genetically Modified Corynebacterium glutamicum—Media and Culture Conditions

[0167]E. coli strains are routinely grown in MB and LB broth, respectively (Follettie, M. T., et al. (1993) J. Bacteriol. 175, 4096-4103). Minimal media for E. coli is M9 and modified MCGC (Yoshihama, M., et al. (1985) J. Bacteriol. 162, 591-507). Glucose was added to a final concentration of 1%. Antibiotics were added in the following amounts (micrograms per milliliter): ampicillin, 50; kanamycin, 25; nalidixic acid, 25. Amino acids, vitamins, and other supplements were added in the following amounts: methionine, 9.3 mM; arginine, 9.3 mM; histidine, 9.3 mM; thiamine, 0.05 mM. E. coil cells were routinely grown at 37° C., respectively.

[0168] Genetically modified Corynebacteria are cultured in synthetic or natural growth media. A number of different growth media for Corynebacteria are both well-known and readily available (Lieb et al. (1989) Appl. Microbiol. Biotechnol., 32:205-210; von der Osten et al. (1998) Biotechnology Letters, 11:11-16; U.S. Pat. No. DE 4,120,867; Liebl (1992) “The Genus Corynebacterium, in: The Procaryotes, Volume II, Balows, A. et al., eds. Springer-Verlag). These media consist of one or more carbon sources, nitrogen sources, inorganic salts, vitamins and trace elements. Preferred carbon sources are sugars, such as mono-, di-, or polysaccharides. For example, glucose, fructose, mannose, galactose, ribose, sorbose, ribulose, lactose, maltose, sucrose, raffinose, starch or cellulose serve as very good carbon sources. It is also possible to supply sugar to the media via complex compounds such as molasses or other by-products from sugar refinement. It can also be advantageous to supply mixtures of different carbon sources. Other possible carbon sources are alcohols and organic acids, such as methanol, ethanol, acetic acid or lactic acid. Nitrogen sources are usually organic or inorganic nitrogen compounds, or materials which contain these compounds. Exemplary nitrogen sources include ammonia gas or ammonia salts, such as NH₄Cl or (NH₄)₂SO₄, NH₄OH, nitrates, urea, amino acids or complex nitrogen sources like corn steep liquor, soy bean flour, soy bean protein, yeast extract, meat extract and others.

[0169] The overproduction of sulfur containing amino acids like homocysteine and methionine was made possible using different sulfur sources. Sulfates, thiosulfates, sulfites and also more reduced sulfur sources like H₂S and sulfides and derivatives can be used. Also, organic sulfur sources like methyl mercaptan, thioglycolates, thiocyanates, thiourea, sulfur containing amino acids like cysteine and other sulfur containing compounds can be used to achieve homocysteine and methionine overproduction

[0170] Inorganic salt compounds which may be included in the media include the chloride-, phosphorous- or sulfate- salts of calcium, magnesium, sodium, cobalt, molybdenum, potassium, manganese, zinc, copper and iron. Chelating compounds can be added to the medium to keep the metal ions in solution. Particularly useful chelating compounds include dihydroxyphenols, like catechol or protocatechuate, or organic acids, such as citric acid. It is typical for the media to also contain other growth factors, such as vitamins or growth promoters, examples of which include biotin, riboflavin, thiamin, folic acid, nicotinic acid, pantothenate and pyridoxin. Growth factors and salts frequently originate from complex media components such as yeast extract, molasses, corn steep liquor and others. The exact composition of the media compounds depends strongly on the immediate experiment and is individually decided for each specific case. Information about media optimization is available in the textbook “Applied Microbiol. Physiology, A Practical Approach (eds. P. M. Rhodes, P. F. Stanbury, IRL Press (1997) pp. 53-73, ISBN 019 963577 3). It is also possible to select growth media from commercial suppliers, like standard 1 (Merck) or BHI (grain heart infusion, DIFCO) or others.

[0171] All medium components are sterilized, either by heat (20 minutes at 1.5 bar and 121° C.) or by sterile filtration. The components can either be sterilized together or, if necessary, separately. All media components can be present at the beginning of growth, or they can optionally be added continuously or batchwise.

[0172] Culture conditions are defined separately for each experiment. The temperature should be in a range between 15° C. and 45° C. The temperature can be kept constant or can be altered during the experiment. The pH of the medium should be in the range of 5 to 8.5, preferably around 7.0, and can be maintained by the addition of buffers to the media. An exemplary buffer for this purpose is a potassium phosphate buffer. Synthetic buffers such as MOPS, HEPES, ACES and others can alternatively or simultaneously be used. It is also possible to maintain a constant culture pH through the addition of NaOH or NHOH during growth. If complex medium components such as yeast extract are utilized, the necessity for additional buffers may be reduced, due to the fact that many complex compounds have high buffer capacities. If a fermentor is utilized for culturing the microorganisms, the pH can also be controlled using gaseous ammonia.

[0173] The incubation time is usually in a range from several hours to several days. This time is selected in order to permit the maximal amount of product to accumulate in the broth. The disclosed growth experiments can be carried out in a variety of vessels, such as microtiter plates, glass tubes, glass flasks or glass or metal fermentors of different sizes. For screening a large number of clones, the microorganisms should be cultured in microtiter plates, glass tubes or shake flasks, either with or without baffles. Preferably 100 ml shake flasks are used, filled with 10% (by volume) of the required growth medium. The flasks should be shaken on a rotary shaker (amplitude 25 mm) using a speed-range of 100-300 rpm. Evaporation losses can be diminished by the maintenance of a humid atmosphere; alternatively, a mathematical correction for evaporation losses should be performed.

[0174] If genetically modified clones are tested, an unmodified control clone or a control clone containing the basic plasmid without any insert should also be tested. The medium is inoculated to an OD₆₀₀ of 0.5-1.5 using cells grown on agar plates, such as CM plates (10 g/l glucose, 2,5 g/l NaCl, 2 g/l urea, 10 g/l polypeptone, 5 g/l yeast extract, 5 g/l meat extract, 22 g/l NaCl, 2 g/l urea, 10 g/l polypeptone, 5 g/l yeast extract, 5 g/l meat extract, 22 g/l agar, pH 6.8 with 2M NaOH) that had been incubated at 30° C. Inoculation of the media is accomplished by either introduction of a saline suspension of C. glutamicum cells from CM plates or addition of a liquid preculture of this bacterium.

EXAMPLE 8

[0175] In vitro Analysis of the Function of Mutant Proteins

[0176] The determination of activities and kinetic parameters of enzymes is well established in the art. Experiments to determine the activity of any given altered enzyme must be tailored to the specific activity of the wild-type enzyme, which is well within the ability of one of ordinary skill in the art. Overviews about enzymes in general, as well as specific details concerning structure, kinetics, principles, methods, applications and examples for the determination of many enzyme activities may be found, for example, in the following references: Dixon, M., and Webb, E. C., (1979) Enzymes. Longmans: London; Fersht, (1985) Enzyme Structure and Mechanism. Freeman: New York; Walsh, (1979) Enzymatic Reaction Mechanisms. Freeman: San Francisco; Price, N. C., Stevens, L. (1982) Fundamentals of Enzymology. Oxford Univ. Press: Oxford; Boyer, P. D., ed. (1983) The Enzymes, 3^(rd) ed. Academic Press: New York; Bisswanger, H., (1994) Enzymkinetik, 2^(nd) ed. VCH: Weinheim (ISBN 3527300325); Bergmeyer, H. U., Bergmeyer, J., Graβl, M., eds. (1983-1986) Methods of Enzymatic Analysis, 3^(rd) ed., vol. I-XII, Verlag Chemie: Weinheim; and Ullmann's Encyclopedia of Industrial Chemistry (1987) vol. A9, “Enzymes”. VCH: Weinheim, p. 352-363.

[0177] Cell extracts from Corynebacterium glutamicum were prepared as described previously (Park, S.-D., et al. (1998) Mol. Cells 8, 286-294). Cystathionine β-lyase was assayed as follows. The assay mixture contained 100 mM Tris-HCl (pH8.5), 0.1 mM NADH, 1 mM L-cystathionine, 5 units of L-lactate dehydrogenase, and appropriate amounts of crude extract. Optical changes were monitored at 340 nm. Assay for S-(□-aminoethyl)-cysteine (AEC) resistance was carried out as described in Rossol, I. and Pühler, A. (1992) J. Bacteriol. 174, 2968-77. The results of cystathionin β-lyase assays from extracts of different Corynebacterium glutamicum strains as well as results of AEC resistance assays of the same strain are summarized in Table 5, below. TABLE 5 Expression of cystathionine β-lyase^(a) Activity Growth on Resistance Strains Properties (nmol min⁻¹ mg ⁻¹) MM^(b) to AEC^(c) C. glutamicum ASO19E12 — 146 + + C. glutamicum ASO19E12/pMT1 Empty vector 145 + + C. glutamicum ASO19E12/pSL173 metC clone 797 + + + C. glutamicum HL457 metC mutant^(d) 19 + − C. glutamicum HL459 metC mutant^(d) 23 + − E. coli JE6839 metC mutant 21 − ND^(e)

[0178] The ability of the metC clones to express cystathionine β-lyase was tested by enzymatic assay. Crude extracts prepared from the C. glutamicum ASO19E12 cells harboring plasmid pSL173 were assayed. Cells harboring the plasmid showed approximately a 5-fold increase in the activity of cystathionine β-lyase compared to those harboring the empty vector pMT1 (Table 5), apparently due to the gene-dose effect. SDS-PAGE analysis of crude extracts revealed a putative cystathionine β-lyase band with approximate M_(r) of 41,000. Intensity of each putative cystathionine β-lyase band agreed with the complementation and enzymatic assay data (Table 5). As described above, a region of metC appeared to be nearly identical to the previously reported aecD. Since the aecD gene was isolated on the basis of its ability to confer resistance to S-(β-aminoethyl)-cysteine (AEC), a toxic lysine analogue, we tested the protein product of metC for the presence of the activity. As shown in Table 5, cells overexpressing cystathionine β-lyase showed increased resistance to AEC. The strain carrying a mutation in metC gene (see below) completely lost its ability to show a resistant phenotype to AEC.

[0179] Assay for O-acetylhmoserine sulphydrylase was performed as follows (Belfaiza, J., et al. (1998) J. Bacteriol. 180, 250-255; Ravanel, S., M. Droux, and R. Douce (1995) Arch. Biochem. Biophys. 316, 572-584; Foglino, M. (1995) Microbiology 141, 431-439). Assay mixture of 0.1 ml contained 20 mM MOPS-NaOH (pH7.5), 10 mM O-acetylhomoserine, 2 mM Na₂S in 50 mM NaOH, and an appropriate amount of enzyme. Immediately after the addition of Na₂S which was added last, the reaction mixture was overlayed with 50 ul of mineral oil. After 30 minute incubation at 30° C., the reaction was stopped by boiling the mixture for 3 minutes. Homocysteine produced in the reaction was quantified as previously described (Yamagata, S. (1987) Method Enzymol. 143, 478-483.). Reaction mixture of 0.1 ml was taken and mixed with 0.1 ml of H₂O, 0.6 ml of saturated NaCl, 0.1 ml of 1.5 M Na₂CO₃ containing 67 mM KCN, and 0.1 ml of 2% nitroprusside. After 1 minute incubation at room temperature, optical density was measured at 520 nm. Corynebacterium cells harboring additional copies of the metZ gene, e.g., a plasmid containing the metZ gene, exhibited significantly higher metZ enzyme activities than the same type of Corynebacterium cells without additional copies of the metZ gene.

[0180] The activity of proteins which bind to DNA can be measured by several well-established methods, such as DNA band-shift assays (also called gel retardation assays). The effect of such proteins on the expression of other molecules can be measured using reporter gene assays (such as that described in Kolmar, H. et al. (1995) EMBO J. 14: 3895-3904 and references cited therein). Reporter gene test systems are well known and established for applications in both pro- and eukaryotic cells, using enzymes such as beta-galactosidase, green fluorescent protein, and several others.

[0181] The determination of activity of membrane-transport proteins can be performed according to techniques such as those described in Gennis, R. B. (1989) “Pores, Channels and Transporters”, in Biomembranes, Molecular Structure and Function, Springer: Heidelberg, p. 85-137; 199-234; and 270-322.

EXAMPLE 9

[0182] Analysis of Impact of Mutant Protein on the Production of the Desired Product

[0183] The effect of the genetic modification in C. glutamicum on production of a desired compound (such as an amino acid) can be assessed by growing the modified microorganism under suitable conditions (such as those described above) and analyzing the medium and/or the cellular component for increased production of the desired product (i. e., an amino acid). Such analysis techniques are well known to one of ordinary skill in the art, and include spectroscopy, thin layer chromatography, staining methods of various kinds, enzymatic and microbiological methods, and analytical chromatography such as high performance liquid chromatography (see, for example, Ullman, Encyclopedia of Industrial Chemistry, vol. A2, p. 89-90 and p. 443-613, VCH: Weinheim (1985); Fallon, A. et al., (1987) “Applications of HPLC in Biochemistry” in: Laboratory Techniques in Biochemistry and Molecular Biology, vol. 17; Rehm et al. (1993) Biotechnology, vol. 3, Chapter III: “Product recovery and purification”, page 469-714, VCH: Weinheim; Belter, P. A. et al. (1988) Bioseparations: downstream processing for biotechnology, John Wiley and Sons; Kennedy, J. F. and Cabral, J. M. S. (1992) Recovery processes for biological materials, John Wiley and Sons; Shaeiwitz, J. A. and Henry, J. D. (1988) Biochemical separations, in: Ulmann's Encyclopedia of Industrial Chemistry, vol. B3, Chapter 11, page 1-27, VCH: Weinheim; and Dechow, F. J. (1989) Separation and purification techniques in biotechnology, Noyes Publications.)

[0184] In addition to the measurement of the final product of fermentation, it is also possible to analyze other components of the metabolic pathways utilized for the production of the desired compound, such as intermediates and side-products, to determine the overall efficiency of production of the compound. Analysis methods include measurements of nutrient levels in the medium (e.g., sugars, hydrocarbons, nitrogen sources, phosphate, and other ions), measurements of biomass composition and growth, analysis of the production of common metabolites of biosynthetic pathways, and measurement of gasses produced during fermentation. Standard methods for these measurements are outlined in Applied Microbial Physiology, A Practical Approach, P. M. Rhodes and P. F. Stanbury, eds., IRL Press, p. 103-129; 131-163; and 165-192 (ISBN: 0199635773) and references cited therein.

EXAMPLE 10

[0185] Purification of the Desired Product from C. glutamicum Culture

[0186] Recovery of the desired product from the C. glutamicum cells or supernatant of the above-described culture can be performed by various methods well known in the art. If the desired product is not secreted from the cells, the cells can be harvested from the culture by low-speed centrifugation, the cells can be lysed by standard techniques, such as mechanical force or sonication. The cellular debris is removed by centrifugation, and the supernatant fraction containing the soluble proteins is retained for further purification of the desired compound. If the product is secreted from the C. glutamicum cells, then the cells are removed from the culture by low-speed centrifugation, and the supernate fraction is retained for further purification.

[0187] The supernatant fraction from either purification method is subjected to chromatography with a suitable resin, in which the desired molecule is either retained on a chromatography resin while many of the impurities in the sample are not, or where the impurities are retained by the resin while the sample is not. Such chromatography steps may be repeated as necessary, using the same or different chromatography resins. One of ordinary skill in the art would be well-versed in the selection of appropriate chromatography resins and in their most efficacious application for a particular molecule to be purified. The purified product may be concentrated by filtration or ultrafiltration, and stored at a temperature at which the stability of the product is maximized.

[0188] There are a wide array of purification methods known to the art and the preceding method of purification is not meant to be limiting. Such purification techniques are described, for example, in Bailey, J. E. & Ollis, D. F. Biochemical Engineering Fundamentals, McGraw-Hill: New York (1986).

[0189] The identity and purity of the isolated compounds may be assessed by techniques standard in the art. These include high-performance liquid chromatography (HPLC), spectroscopic methods, staining methods, thin layer chromatography, NIRS, enzymatic assay, or microbiologically. Such analysis methods are reviewed in: Patek et al. (1994) Appl. Environ. Microbiol. 60: 133-140; Malakhova et al. (1996) Biotekhnologiya 11: 27-32; and Schmidt et al. (1998) Bioprocess Engineer. 19: 67-70. Ulmann's Encyclopedia of Industrial Chemistry, (1996) vol. A27, VCH: Weinheim, p. 89-90, p. 521-540, p. 540-547, p. 559-566, 575-581 and p. 581-587; Michal, G. (1999) Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology, John Wiley and Sons; Fallon, A. et al. (1987) Applications of HPLC in Biochemistry in: Laboratory Techniques in Biochemistry and Molecular Biology, vol. 17.

EXAMPLE 11

[0190] Analysis of the Gene Sequences of the Invention

[0191] The comparison of sequences and determination of percent homology between two sequences are art-known techniques, and can be accomplished using a mathematical algorithm, such as the algorithm of Karlin and Altschul (1990) Proc. Natl. Acad. Sci. USA 87:2264-68, modified as in Karlin and Altschul (1993) Proc. Natl. Acad. Sci. USA 90:5873-77. Such an algorithm is incorporated into the NBLAST and XBLAST programs (version 2.0) of Altschul, et al. (1990) J. Mol. Biol. 215:403-10. BLAST nucleotide searches can be performed with the NBLAST program, score=100, wordlength=12 to obtain nucleotide sequences homologous to MP nucleic acid molecules of the invention. BLAST protein searches can be performed with the XBLAST program, score=50, wordlength=3 to obtain amino acid sequences homologous to MP protein molecules of the invention. To obtain gapped alignments for comparison purposes, Gapped BLAST can be utilized as described in Altschul et al., (1997) Nucleic Acids Res. 25(17):3389-3402. When utilizing BLAST and Gapped BLAST programs, one of ordinary skill in the art will know how to optimize the parameters of the program (e.g., XBLAST and NBLAST) for the specific sequence being analyzed.

[0192] Another example of a mathematical algorithm utilized for the comparison of sequences is the algorithm of Meyers and Miller ((1988) Comput. Appl. Biosci. 4: 11-17). Such an algorithm is incorporated into the ALIGN program (version 2.0) which is part of the GCG sequence alignment software package. When utilizing the ALIGN program for comparing amino acid sequences, a PAM120 weight residue table, a gap length penalty of 12, and a gap penalty of 4 can be used. Additional algorithms for sequence analysis are known in the art, and include ADVANCE and ADAM. described in Torelli and Robotti (1994) Comput. Appl. Biosci. 10:3-5; and FASTA, described in Pearson and Lipman (1988) P.N.A.S. 85:2444-8.

[0193] The percent homology between two amino acid sequences can also be accomplished using the GAP program in the GCG software package (available at http://www.gcg.com), using either a Blosum 62 matrix or a PAM250 matrix, and a gap weight of 12, 10, 8, 6, or 4 and a length weight of 2, 3, or 4. The percent homology between two nucleic acid sequences can be accomplished using the GAP program in the GCG software package, using standard parameters, such as a gap weight of 50 and a length weight of 3.

[0194] A comparative analysis of the gene sequences of the invention with those present in Genbank has been performed using techniques known in the art (see, e.g., Bexevanis and Ouellette, eds. (1998) Bioinformatics: A Practical Guide to the Analysis of Genes and Proteins. John Wiley and Sons: New York). The gene sequences of the invention were compared to genes present in Genbank in a three-step process. In a first step, a BLASTN analysis (e.g., a local alignment analysis) was performed for each of the sequences of the invention against the nucleotide sequences present in Genbank, and the top 500 hits were retained for further analysis. A subsequent FASTA search (e.g., a combined local and global alignment analysis, in which limited regions of the sequences are aligned) was performed on these 500 hits. Each gene sequence of the invention was subsequently globally aligned to each of the top three FASTA hits, using the GAP program in the GCG software package (using standard parameters). In order to obtain correct results, the length of the sequences extracted from Genbank were adjusted to the length of the query sequences by methods well-known in the art. The results of this analysis are set forth in Table 4. The resulting data is identical to that which would have been obtained had a GAP (global) analysis alone been performed on each of the genes of the invention in comparison with each of the references in Genbank, but required significantly reduced computational time as compared to such a database-wide GAP (global) analysis. Sequences of the invention for which no alignments above the cutoff values were obtained are indicated on Table 4 by the absence of alignment information. It will further be understood by one of ordinary skill in the art that the GAP alignment homology percentages set forth in Table 4 under the heading “% homology (GAP)” are listed in the European numerical format, wherein a ‘,’ represents a decimal point. For example, a value of “40,345” in this column represents “40.345%”.

EXAMPLE 12

[0195] Construction and Operation of DNA Microarrays

[0196] The sequences of the invention may additionally be used in the construction and application of DNA microarrays (the design, methodology, and uses of DNA arrays are well known in the art, and are described, for example, in Schena, M. et al. (1995) Science 270: 467-470; Wodicka, L. et al. (1997) Nature Biotechnology 15: 1359-1367; DeSaizieu, A. et al. (1998) Nature Biotechnology 16: 45-48; and DeRisi, J. L. et al. (1997) Science 278: 680-686).

[0197] DNA microarrays are solid or flexible supports consisting of nitrocellulose, nylon, glass, silicone, or other materials. Nucleic acid molecules may be attached to the surface in an ordered manner. After appropriate labeling, other nucleic acids or nucleic acid mixtures can be hybridized to the immobilized nucleic acid molecules, and the label may be used to monitor and measure the individual signal intensities of the hybridized molecules at defined regions. This methodology allows the simultaneous quantification of the relative or absolute amount of all or selected nucleic acids in the applied nucleic acid sample or mixture. DNA microarrays, therefore, permit an analysis of the expression of multiple (as many as 6800 or more) nucleic acids in parallel (see, e.g., Schena, M. (1996) BioEssays 18(5): 427-431).

[0198] The sequences of the invention may be used to design oligonucleotide primers which are able to amplify defined regions of one or more C. glutamicum genes by a nucleic acid amplification reaction such as the polymerase chain reaction. The choice and design of the 5′ or 3′ oligonucleotide primers or of appropriate linkers allows the covalent attachment of the resulting PCR products to the surface of a support medium described above (and also described, for example, Schena, M. et al. (1995) Science 270: 467-470).

[0199] Nucleic acid microarrays may also be constructed by in situ oligonucleotide synthesis as described by Wodicka, L. et al (1997) Nature Biotechnology 15: 1359-1367. By photolithographic methods, precisely defined regions of the matrix are exposed to light. Protective groups which are photolabile are thereby activated and undergo nucleotide addition, whereas regions that are masked from light do not undergo any modification. Subsequent cycles of protection and light activation permit the synthesis of different oligonucleotides at defined positions. Small, defined regions of the genes of the invention may be synthesized on microarrays by solid phase oligonucleotide synthesis.

[0200] The nucleic acid molecules of the invention present in a sample or mixture of nucleotides may be hybridized to the microarrays. These nucleic acid molecules can be labeled according to standard methods. In brief, nucleic acid molecules (e.g., mRNA molecules or DNA molecules) are labeled by the incorporation of isotopically or fluorescently labeled nucleotides, e.g., during reverse transcription or DNA synthesis. Hybridization of labeled nucleic acids to microarrays is described (e.g., in Schena, M. et al. (1995) supra; Wodicka, L. et al. (1997), supra; and DeSaizieu A. et al. (1998), supra). The detection and quantification of the hybridized molecule are tailored to the specific incorporated label. Radioactive labels can be detected, for example, as described in Schena, M. et al. (1995) supra) and fluorescent labels may be detected, for example, by the method of Shalon et al. (1996) Genome Research 6: 639-645).

[0201] The application of the sequences of the invention to DNA microarray technology, as described above, permits comparative analyses of different strains of C. glutamicum or other Corynebacteria. For example, studies of inter-strain variations based on individual transcript profiles and the identification of genes that are important for specific and/or desired strain properties such as pathogenicity, productivity and stress tolerance are facilitated by nucleic acid array methodologies. Also, comparisons of the profile of expression of genes of the invention during the course of a fermentation reaction are possible using nucleic acid array technology.

EXAMPLE 13

[0202] Analysis of the Dynamics of Cellular Protein Populations (Proteomics)

[0203] The genes, compositions, and methods of the invention may be applied to study the interactions and dynamics of populations of proteins, termed ‘proteomics’. Protein populations of interest include, but are not limited to, the total protein population of C. glutamicum (e.g., in comparison with the protein populations of other organisms), those proteins which are active under specific environmental or metabolic conditions (e.g., during fermentation, at high or low temperature, or at high or low pH), or those proteins which are active during specific phases of growth and development.

[0204] Protein populations can be analyzed by various well-known techniques, such as gel electrophoresis. Cellular proteins may be obtained, for example, by lysis or extraction, and may be separated from one another using a variety of electrophoretic techniques. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) separates proteins largely on the basis of their molecular weight. Isoelectric focusing polyacrylamide gel electrophoresis (IEF-PAGE) separates proteins by their isoelectric point (which reflects not only the amino acid sequence but also posttranslational modifications of the protein). Another, more preferred method of protein analysis is the consecutive combination of both IEF-PAGE and SDS-PAGE, known as 2-D-gel electrophoresis (described, for example, in Hermann et al. (1998) Electrophoresis 19: 3217-3221; Fountoulakis et al. (1998) Electrophoresis 19: 1193-1202; Langen et al. (1997) Electrophoresis 18: 1184-1192; Antelmann et al. (1997) Electrophoresis 18: 1451-1463). Other separation techniques may also be utilized for protein separation, such as capillary gel electrophoresis; such techniques are well known in the art.

[0205] Proteins separated by these methodologies can be visualized by standard techniques, such as by staining or labeling. Suitable stains are known in the art, and include Coomassie Brilliant Blue, silver stain, or fluorescent dyes such as Sypro Ruby (Molecular Probes). The inclusion of radioactively labeled amino acids or other protein precursors (e.g., ³⁵S-methionine, ³⁵S-cysteine, ¹⁴C-labelled amino acids, ¹⁵N-amino acids, ¹⁵NO₃ or ¹⁵NH₄ ⁺ or ¹³C-labelled amino acids) in the medium of C. glutamicum permits the labeling of proteins from these cells prior to their separation. Similarly, fluorescent labels may be employed. These labeled proteins can be extracted, isolated and separated according to the previously described techniques.

[0206] Proteins visualized by these techniques can be further analyzed by measuring the amount of dye or label used. The amount of a given protein can be determined quantitatively using, for example, optical methods and can be compared to the amount of other proteins in the same gel or in other gels. Comparisons of proteins on gels can be made, for example, by optical comparison, by spectroscopy, by image scanning and analysis of gels, or through the use of photographic films and screens. Such techniques are well-known in the art.

[0207] To determine the identity of any given protein, direct sequencing or other standard techniques may be employed. For example, N- and/or C-terminal amino acid sequencing (such as Edman degradation) may be used, as may mass spectrometry (in particular MALDI or ESI techniques (see, e.g., Langen et al. (1997) Electrophoresis 18: 1184-1192)). The protein sequences provided herein can be used for the identification of C. glutamicum proteins by these techniques.

[0208] The information obtained by these methods can be used to compare patterns of protein presence, activity, or modification between different samples from various biological conditions (e.g., different organisms, time points of fermentation, media conditions, or different biotopes, among others). Data obtained from such experiments alone, or in combination with other techniques, can be used for various applications, such as to compare the behavior of various organisms in a given (e.g., metabolic) situation, to increase the productivity of strains which produce fine chemicals or to increase the efficiency of the production of fine chemicals.

EXAMPLE 14

[0209] Cloning of Genes by Application of the Polymerase Chain Reaction (PCR)

[0210] Genes can be amplified using specific oligonucleotides comprising either nucleotide sequences homologous to sequences of Corynebacterium glutamicum or other strains as well as recognition sites of restriction enzymes well known in the art (e.g., as described in Sambrook, J., Fritsh, E. F., and Maniatis, T. Molecular Cloning: A Laboratory Manual. 2nd, ed., Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1989). Theses oligonucleotides can be used to amplify specific DNA-fragments containing parts of the chromosome of mentioned strains using DNA-polymerases such as T. aquaticus DNA-polymerase, P. furiosus DNA-polymerase, or P. woesei DNA-polymerase and dNTPs nucleotides in an appropriate buffer solution as described by the manufacturer.

[0211] Gene fragments such as coding sequences from RXA00657 including appropriate upstream and downstream regions not contained in the coding region of the mentioned gene can be amplified using the aforementioned technologies. Furthermore, these fragments can be purified from unincorporated oligonucleotides and nucleotides. DNA restriction enzymes can be used to produce protruding ends that can be used to ligate DNA fragments to vectors digested with complementary enzymes or compatible enzymes producing ends that can be used to ligate the DNA into the vectors mentioned in Sinskey et al., U.S. Pat. No. 4,649,119, and techniques for genetic manipulation of C. glutamicum and the related Brevibacterium species (e.g., lactofermentum) (Yoshihama et al, J. Bacteriol. 162: 591-597 (1985); Katsumata et al., J. Bacteriol. 159: 306-311 (1984); and Santamaria et al., J. Gen. Microbiol. 130: 2237-2246 (1984). Oligonucleotides used as primers for the amplification of upstream DNA sequence, the coding region sequence and the downstream region of RXA00657 were as follows: TCGGGTATCCGCGCTACACTTAGA (SEQ ID NO:121); GGAAACCGGGGCATCGAAACTTA (SEQ ID NO:122).

[0212]Corynebacterium glutamicum chromosomal DNA with an amount of 200 ng was used as a template in a 100 μl reaction volume containing 2,5U Pfu Turbo-Polymerase™ (Stratagene™), and 200 μM dNTP-nucleotides The PCR was performed on a PCR-Cycler™ (Perkin Elmer 2400™) using the following temperature/time protocol:

[0213] 1 cycle: 94° C.: 2 min.;

[0214] 20 cycle: 94° C.: 1 min.;

[0215] 52° C.: 1 min, 72° C.: 1.5 min.,

[0216] 1 cycle: 72° C.: 5 min.

[0217] Primers were removed from the resulting amplified DNA fragment and the resulting fragment was cloned into the blunt EcoRV site of pBS KS (Stratagene™). The fragment was excised by digestion with the restriction enzymes BamHI/XhoI and ligated into a BamHI SalI digested vector pB (SEQ ID NO.:125). The resulting vector is called pB RXA00657.

[0218] Resulting recombinant vectors can be analyzed using standard techniques described in e.g., Sambrook, J., Fritsh, E. F., and Maniatis, T. Molecular Cloning: A Laboratory Manual. 2nd, ed., Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., 1989), and can be transferred into C. glutamicum using aforementioned techniques.

[0219] A Corynebacterium strain (ATCC 13286) was treated for a transformation as described. Transformation of C. glutamicum can be achieved by protoplast transformation (Kastsumata, R. et al. (1984) J. Bacteriol. 159306-311), electroporation (Liebl, E. et al. (1989) FEMS Microbiol. Letters, 53:399-303) and in cases where special vectors are used, also by conjugation (as described, e.g., in Schafer, A. et al. (1990) J. Bacteriol. 172:1663-1666). It is also possible to transfer the shuttle vectors for C. glutamicum to E. coli by preparing plasmid DNA from C. glutamicum (using standard methods well-known in the art) and transforming it into E. coli. This transformation step can be performed using standard methods, but it is advantageous to use an Mcr-deficient E. coli strain, such as NM522 (Gough & Murray (1983) J. Mol. Biol. 166:1-19).

[0220] Transformation of a bacterial strain such as Corynebacterium glutamicum strain (ATCC 13286) was performed with a plasmid pB containing the aforementioned DNA regions of RXA00657 (SEQ ID NO.:6) and in another case with the vector pB (SEQ ID NO.: ) carrying no additional insertion of nucleic acids.

[0221] The resulting strains were plated on and isolated from CM-Medium (10 g/l Glucose 2,5 g/l NaCl, 2,0 g/l Urea, 10 g/l Bacto Peptone (Difco/Becton Dicinson/Sparks USA™), 5 g/l yeast extract (Difco/Becton Dicinson/Sparks USA™), 5g/l meat extract (Difco/Becton Dicinson/Sparks USA™), 22g/l Agar (Difco/Becton Dickinson/Sparks USA™) and 15 μg/ml kanamycin sulfate (Serva, Germany) with a adjusted with NaOH to pH of 6.8.

[0222] Strains isolated from the aforementioned agar medium were inoculated in 10 ml in a 100ml shake flask containing no baffles in liquid medium containing 100 g/l sucrose 50 g/l (NH4)₂SO₄, 2,5 g/l NaCl, 2,0 g/l Urea, 10 g/l Bacto Peptone (Difco/Becton Dickinson/Sparks USA), 5 g/l yeast extract (Difco/Becton Dickinson/Sparks USA), 5 g/l meat extract (Difco/Becton Dickinson/Sparks USA), and 25 g/l CaCO3 (Riedel de Haen, Germany). Medium was a adjusted with NaOH to pH of 6.8.

[0223] Strains were incubated at 30° C. for 48 h. Supernatants of incubations were prepared by centrifugation 20′ at 12,000 rpm in an Eppendorf™ microcentrifuge. Liquid supernatants were diluted and subjected to amino acid analysis (Standard methods for these measurements are outlined in Applied Microbial Physiology, A Practical Approach, P. M. Rhodes and P. F. Stanbury, eds., IRL Press, p. 103-129; 131-163; and 165-192 (ISBN: 0199635773) and references cited therein).

[0224] The results are shown in Table 6, below. TABLE 6 RESULTS: Strain ATCC Plasmid 13286 contained pB pB RXA00657 lysin produced 13.5 14.93 (g/l) Selectivity 0.235 0.25 (mol lysine/ mol consumed Saccharose)

[0225] Equivalents

[0226] Those of ordinary skill in the art will recognize, or will be able to ascertain using no more than routine experimentation, many equivalents to the specific embodiments of the invention described herein. Such equivalents are intended to be encompassed by the following claims. TABLE 1 Included Genes Nucleic Acid SEQ ID Amino Acid Identification NO SEQ ID NO Code Contig. NT Start NT Stop Function Lysine biosynthesis 5 6 RXA00657 AMINOACID BIOSYNTHESIS REGULATOR 7 8 RXA02229 GR00653 2793 3617 DIAMINOPIMELATE EPIMERASE (EC 5.1.1.7) 9 10 RXS02970 ACETYLORNITHINE AMINOTRANSFERASE (EC 2.6.1.11) 11 12 F RXA01009 GR00287 4714 5943 ACETYLORNITHINE AMINOTRANSFERASE (EC 2.6.1.11) 13 14 RXC02390 MEMBRANE SPANNING PROTEIN INVOLVED IN LYSINE META- BOLISM 15 16 RXC01796 MEMBRANE ASSOCIATED PROTEIN INVOLVED IN LYSINE METABOLISM 17 18 RXC01207 CYTOSOLIC PROTEIN INVOLVED IN METABOLISM OF LYSINE AND THREONINE 19 20 RXC00657 TRANSCRIPTIONAL REGULATOR INVOLVED IN LYSINE METABOLISM 21 22 RXC00552 CYTOSOLIC PROTEIN INVOLVED IN LYSINE METABOLISM 23 24 RXA00534 GR00137 4758 3496 ASPARTOKINASE ALPHA AND BETA SUBUNITS (EC 2 7.2.4) 25 26 RXA00533 GR00137 3469 2438 ASPARTATE-SEMIALDEHYDE DEHYDROGENASE (EC 1.2.1.11) 27 28 RXA02843 GR00842 543 4 2,3,4,5-TETRAHYDROPYRIDINE-2-CARBOXYLATE N-SUCCINYLTRANSFERASE (EC 2.3 1.117) 29 30 RXA02022 GR00613 2063 3169 SUCCINYL-DIAMINOPIMELATE DESUCCINYLASE (EC 3.5.1.18) 31 32 RXA00044 GR00007 3458 4393 DIHYDRODIPICOLINATE SYNTHASE (EC 4.2.1.52) 33 34 RXA00863 GR00236 896 1639 DIHYDRODIPICOLINATE REDUCTASE (EC 1 3.1.26) 35 36 RXA00864 GR00236 1694 2443 probable 2,3-dihydrodipicolinate N-C6-lyase (cyclizing) (EC 4.3.3.−) - Corynebacterium glutamicum 37 38 RXA02843 GR00842 543 4 2,3,4,5-TETRAHYDROPYRIDINE-2-CARBOXYLATE N-SUCCINYLTRANSFERASE (EC 2.3.1.117) 39 40 RXN00355 VV0135 31980 30961 MESO-DIAMINOPIMELATE D-DEHYDROGENASE 41 42 F RXA00352 GR00068 861 4 MESO-DIAMINOPIMELATE D-DEHYDROGENASE (EC 1.4.1.16) 43 44 RXA00972 GR00274 3 1379 DIAMINOPIMELATE DECARBOXYLASE (EC 4.1.1.20) 45 46 RXA02653 GR00752 5237 7234 DIAMINOPIMELATE DECARBOXYLASE (EC 4.1.1.20) 47 48 RXA01393 GR00408 4249 3380 LYSINE EXPORT REGULATOR PROTEIN 49 50 RXA00241 GR00036 5443 6945 L-LYSINE TRANSPORT PROTEIN 51 52 RXA01394 GR00408 4320 5018 LYSINE EXPORTER PROTEIN 53 54 RXA00865 GR00236 2647 3549 DIHYDRODIPICOLINATE SYNTHASE (EC 4.2.1.52) 55 56 RXS02021 2,3,4,5-TETRAHYDROPYRIDINE-2-CARBOXYLATE N-SUCCINYLTRANSFERASE (EC 2.3 1.117) 57 58 RXS02157 ACETYLORNITHINE AMINOTRANSFERASE (EC 2.6.1.11) 59 60 RXC00733 ABC TRANSPORTER ATP-BINDING PROTEIN INVOLVED IN LYSINE METABOLISM 61 62 RXC00861 PROTEIN INVOLVED IN LYSINE METABOLISM 63 64 RXC00866 ZN-DEPENDENT HYDROLASE INVOLVED IN LYSINE METABOLISM 65 66 RXC02095 ABC TRANSPORTER ATP-BINDING PROTEIN INVOLVED IN LYSINE METABOLISM 67 68 RXC03185 PROTEIN INVOLVED IN LYSINE METABOLISM Metabolism of methionine and S-adenosyl methionine 1 2 metZ or met O-ACETYLHOMOSERINE SULFHYDRYLASE (EC 4.2.99.10) 3 4 metC Cystathionine-y-lyase 69 70 RXA00115 GR00017 5359 4313 HOMOSERINE O-ACETYLTRANSFERASE (EC 2.3.1.31) 71 72 RXN00403 VV0086 70041 68911 HOMOSERINE O-ACETYLTRANSFERASE 73 74 F RXA00403 GR00088 723 1832 HOMOSERINE O-ACETYLTRANSFERASE (EC 2.3.1.11) 75 76 RXS03158 CYSTATHIONINE GAMMA-SYNTHASE (EC 4.2.99.9) 77 78 F RXA00254 GR00038 2404 1811 CYSTATHIONINE GAMMA-SYNTHASE (EC 4.2.99.9) 79 80 RXA02532 GR00726 3085 2039 CYSTATHIONINE GAMMA-SYNTHASE (EC 4.2.99.9) 81 82 RXS03159 CYSTATHIONINE GAMMA-SYNTHASE (EC 4.2.99.9) 83 84 F RXA02768 GR00770 1919 2521 CYSTATHIONINE GAMMA-SYNTHASE (EC 4.2.99.9) 85 86 RXA00216 GR00032 16286 15297 5-methyltetrahydrofolate-homocysteine methyltransferase (methionine synthetase) 87 94 RXA02197 GR00645 4552 4025 5-METHYLTETRAHYDROFOLATE-HOMOCYSTEINE METHYLTRANSFERASE (EC 2.1.1.13) 89 90 RXN02198 VV0302 9228 11726 5-METHYLTETRAHYDROFOLATE-HOMOCYSTEINE METHYLTRANSFERASE (EC 2.1.1.13) 91 91 F RXA02198 GR00646 2483 6 5-METHYLTETRAHYDROFOLATE-HOMOCYSTEINE METHYLTRANSFERASE (EC 2.1.1.13) 93 94 RXN03074 VV0042 2238 1741 S-ADENOSYLMETHIONINE:2-DEMETHYLMENAQUINONE METHYLTRANSFERASE (EC 2.1.−.−) 95 96 F RXA02906 GR10044 1142 645 S-ADENOSYLMETHIONINE:2-DEMETHYLMENAQUINONE METHYLTRANSFERASE (EC 2.1.−.−) 97 98 RXN00132 VV0124 3612 5045 ADENOSYLHOMOCYSTEINASE (EC 3.3.1.1) 99 100 F RXA00132 GR00020 7728 7624 ADENOSYLHOMOCYSTEINASE (EC 3.3.1.1) 101 102 F RXA01371 GR00398 2339 3634 ADENOSYLHOMOCYSTEINASE (EC 3.3.1.1) 103 104 RXN02085 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE- HOMOCYSTEINE METHYLTRANSFERASE (EC 2.1.1.14) 105 106 F RXA02085 GR00629 3496 5295 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE- HOMOCYSTEINE METHYLTRANSFERASE (EC 2.1.1.14) 107 108 F RXA02086 GR00629 5252 5731 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE- HOMOCYSTEINE METHYLTRANSFERASE (EC 2.1.1.14) 109 110 RXN02648 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE- HOMOCYSTEINE METHYLTRANSFERASE (EC 2.1.1.14) 111 112 F RXA02648 GR00751 5254 4730 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE- HOMOCYSTEINE METHYLTRANSFERASE (EC 2.1.1.14) 113 114 F RXA02658 GR00752 14764 15447 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE- HOMOCYSTEINE METHYLTRANSFERASE (EC 2.1.1.14) 115 116 RXC02238 PROTEIN INVOLVED IN METABOLISM OF S-ADENOSYLMETHIONINE, PURINES AND PANTOTHENATE 117 118 RXC00128 EXPORTED PROTEIN INVOLVED IN METABOLISM OF PYRIDIMES AND ADENOSYLHOMOCYSTEINE S-2adenosyl methionine (SAM) Biosynthesis 119 120 RXA02240 GR00654 7160 8380 S-ADENOSYLMETHIONINE SYNTHETASE (EC 2.5.1.6)

[0227] TABLE 2 GENES IDENTIFIED FROM GENBANK GenBank ™ Accession No. Gene Name Gene Function Reference A09073 ppg Phosphoenol pyruvate carboxylase Bachmann, B. et al. “DNA fragment coding for phosphenolpyruvat corboxylase, recombinant DNA carrying said fragment, strains carrying the recombinant DNA and method for producing L-aminino acids using said strains,” Patent: EP 0358940-A 3 03/21/90 A45579, Threonine dehydratase Moeckel, B. et al. “Production of L-isoleucine by means of recombinant A45581, micro-organisms with deregulated threonine dehdratase,” Patent: WO A45583, 9519442-A 5 07/20/95 A45585 A45587 AB003132 murC; ftsQ; ftsZ Kobayashi, M. et al. “Cloning, sequencing, and characterization of the ftsZ gene from coryneform bacteria,” Biochem. Biophys. Res. Commun., 236(2): 383-388 (1997) AB015023 murC; ftsQ Wachi, M. et al. “A murC gene from Coryneform bacteria,” Appl. Microbiol. Biotechnol., 51(2): 223-228 (1999) AB018530 dtsR Kimura, E. et al. “Molecular cloning of a novel gene, dtsR, which rescues the detergent sensitivity of a mutant derived from Brevibacterium lactofermentum,” Biosci. Biotechnol. Biochem., 60(10): 1565-1570 (1996) AB018531 dtsR1; dtsR2 AB020624 murI D-glutamate racemase AB023377 tkt transketolase AB024708 gltB; gltD Glutamine 2-oxoglutarate amino- transferase large and small subunits AB025424 acn aconitase AB027714 rep Replication protein AB027715 rep; aad Replication protein; aminoglycoside adenyltransferase AF005242 argC N-acetylglutamate-5-semialdehyde dehydrogenase AF005635 glnA Glutamine synthetase AF030405 hisF cyclase AF030520 argG Argininosuccinate synthetase AF031518 argF Ornithine carbamolytransferase AF036932 aroD 3-dehydroquinate dehydratase AF038548 pyc Pyruvate carboxylase AF038651 dciAE; apt; rel Dipeptide-binding protein; adenine Wehmeier, L. et al. “The role of the Corynebacterium glutamicum rel gene phosphoribosyltransferase; GTP in (p)ppGpp metabolism,” Microbiology, 144:1853-1862 (1998) pyrophosphokinase AF041436 argR Arginine repressor AF045998 impA Inositol monophosphate phosphatase AF048764 argH Argininosuccinate lyase AF049897 argC; argJ; argB; N-acetylglutamylphosphate reductase; argD; argF; argR; ornithine acetyltransferase; N- argG; argH acetyiglutamate kinase; acetyl- ornithine transminase; ornithine carbamoyltransferase; arginine repressor; argininosuccinate synthase; argininosuccinate lyase AF050109 inhA Enoyl-acyl carrier protein reductase AF050166 hisG ATP phosphoribosyltransferase AF051846 hisA Phosphoribosylformimino-5-amino-1- phosphoribosyl-4-imidazole- carboxamide isomerase AF052652 metA Homoserine O-acetyltransferase Park, S. et al. “Isolation and analysis of metA, a methionine biosynthetic gene encoding homoserine acetyltransferase in Corynebacterium glutamicum,” Mol. Cells., 8(3): 286-294 (1998) AF053071 aroB Dehydroquinate synthetase AF060558 hisH Glutamine amidotransferase AF086704 hisE Phosphoribosyl-ATP- pyrophosphohydrolase AF114233 aroA 5-enolpyruvylshikimate 3-phosphate synthase AF116184 panD L-aspartate-alpha-decarboxylase Dusch, N. et al. “Expression of the Corynebacterium glutamicum panD gene precursor encoding L-aspartate-alpha-decarbozylase leads to pantothenate overproduction in Escherichia coli,” Appl. Environ. Microbiol., 65(4)1530- 1539 (1999) AF124518 aroD; aroE 3-dehydroquinase; shikimate dehydrogenase AF124600 aroC; aroK; aroB; Chorismate synthase; shikimate pepQ kinase; 3-dehydroquinate synthase; putative cytoplasmic peptidase AF145897 inhA AF145898 inhA AJ001436 ectP Transport of ectoine, glycine betaine, Peter, H. et al. “Corynebacterium glutamicum is equipped with four proline secondary carriers for compatible solutes: Identification, sequencing, and characterization of the proline/ectoine uptake system ProP, and the ectoine/ proline/glycine betaine carrier, EctP,” J. Bacteriol., 180(22): 6005-6012 (1998) AJ004934 dapD Tetrahydrodipicolinate succinylase Wehrmann, A. et al. “Different modes of diaminopimelate synthesis and (incomplete^(i)) their role in cell wall integrity: A study with Corynebacterium glutamicum,” J. Bacteriol., 180(12): 3159-3165 (1998) AJ007732 ppc; secG; amt; Phosphoenolpyruvate-carboxylase; ?; ocd; soxA high affinity ammonium uptake protein; putative ornithine-cyclode- carboxylase; sarcosine oxidase AJ010319 ftsY, glnB, glnD; Involved in cell division; PII protein; Jakoby, M. et al. “Nitrogen regulation in Corynebacterium glutamicum; srp; amtP uridylyltransferase (uridylyl- Isolation of genes involved in biochemical characterization of corresponding removing enzmye); signal recognition proteins,” FEMS Microbiol., 173(2): 303-310 (1999) particle; low affinity ammonium uptake protein AJ132968 cat Chloramphenicol aceteyl transferase AJ224946 mqo L-malate: quinone oxidoreductase Molenaar, D. et al. “Biochemical and genetic characterization of the membrane-associated malate dehydogenase (acceptor) from Corynebacterium glutamicum,” Eur. J. Biochem., 254(2): 395-403 (1998) AJ238250 ndh NADH dehydrogenase AJ238703 porA Porin Lichtinger, T. et al. “Biochemical and biophysical characterization of the cell wall porin of Corynebacterium glutamicum; The channel is formed by a low molecular mass polypeptide,” Biochemistry, 37(43): 15024-15032 (1998) D17429 Transposable element IS31831 Vertes et al. “Isolation and characterization of IS31831, a transposable element from Corynebacterium glutamicum,” Mol Micobiol., 11(4): 739- 746 (1994) D84102 odhA 2-oxoglutarate dehydrogenase Usuda, Y. et al. “Molecular cloning of the Corynebacterium glutamicum (Brevibacterium lactofermentum AJ12036) odhA gene encoding a novel type of 2-oxoglutarate dehydrogenase,” Microbiology, 143:3347-3354 (1996) E01358 hdh; hk Homoserine dehydrogenase; Katsumata, R. et al. “Production of L-thereonine and L-isoleucine,” Patent: homoserine kinase JP 1987232392-A 1 10/12/87 E01359 Upstream of the start codon of Katsumata, R. et al. “Production of L-thereonine and L-isoleucine,” Patent: homoserine kinase gene JP 1987232392-A 2 10/12/87 E01375 Tryptophan operon E01376 trpL; trpE Leader peptide; anthranilate synthase Matsui, K. et al. “Tryptophan operon, peptide and protein coded therby, utilization of tryptophan operon gene expression and production of tryptophan,” Patent: JP 1987244382-A 1 10/24/87 E01377 Promoter and operator regions of Matsui, K. et al. “Tryptophan operon, peptide and protein coded thereby, tryptophan operon utilization of tryptophan operon gene expression and production of tryptophan,” Patent: JP 1987244382-A 1 10/24/87 E03937 Biotin-synthase Hatakeyama, K. et al. “DNA fragment containing gene capable of coding biotin synthetase and its utilization,” Patent: JP 1992278088-A 1 10/02/92 E04040 Diamino pelargonic acid Kohama, K. et al. “Gene coding diaminoperlargonic acid aminotransferase aminotransferase and desthiobiotin synthetase and its utilization,” Patent: JP 1992330284-A 1 11/18/92 E04041 Desthiobiotinsynthetase Kohama, K. et al. “Gene coding diaminoperlargonic acid aminotransferase and desthiobiotin synthetase and its utilization,” Patent: JP 1992330284-A 1 11/18/92 E04307 Flavum aspartase Kurusu, Y. et al. “Gene DNA coding aspartase and utilization thereof,” Patent: JP 1993030977-A 1 02/09/93 E04376 Isocitric acid lyase Katsumata, R. et al. “Gene manifestation controlling DNA,” Patent: JP 1993056782-A 3 03/09/93 E04377 Isocitric acid lyase N-terminal Katsumata, R. et al. “Gene manifestation controlling DNA,” Patent: JP fragment 1993056782-A 3 03/09/93 E04484 Prephenate dehydratase Sotouchi, N. et al. “Production of L-phenylalanine by fermentation,” Patent: JP 1993076352-A 2 03/30/93 E05108 Aspartokinase Fugono, N. et al. “Gene DNA coding Aspartokinase and its use,” Patent: JP 1993184366-A 1 07/27/93 E05112 Dihydro-dipichorinate synthetase Hatakeyama, K. et al. “Gene DNA coding dihydrodipicolinic acid synthetase and its use,” Patent: JP 1993184371-A 1 07/27/93 E05776 Diaminopimelic acid dehydrogenase Kobayashi, M. et al. “Gene DNA coding Daminopimelic acid dehydrogenase and its use,” Patent: JP 1993284970-A 1 11/02/93 E05779 Threonine synthase Kohama, K. et al. “Gene DNA coding threonine synthase and its use,” Patent: JP 1993284972-A 1 11/02/93 E06110 Prephenate dehydratase Kikuchi, T. et al. “Production of L-phenylalanine by fermentation method,” Patent: JP 1993344881-A 1 12/27/93 E06111 Mutated Prephenate dehydratase Kikuchi, T. et al. “Production of L-phenylalanine by fermentation method,” Patent: JP 1993344881-A 1 12/27/93 E06146 Acetohydroxy acid synthetase Inui, M. et al. “Gene capable of coding Acetohydroxy acid synthetase and its use,” Patent: JP 1993344893-A 1 12/27/93 E06825 Aspartokinase Sugimoto, M. et al. “Mutant aspartokinase gene,” patent: JP 1994062866- A 1 03/08/94 E06826 Mutated aspartokinase alpha subunit Sugimoto, M. et al. “Mutant aspartokinase gene,” patent: JP 1994062866- A 1 03/08/94 E06827 Mutated aspartokinase alpha subunit Sugimoto, M. et al. “Mutant aspartokinase gene,” patent: JP 1994062866- A 1 03/08/94 E07701 secY Honno, N. et al. “Gene DNA participating in integration of membraneous protein to membrane,” Patent: JP 1994169780-A 1 06/21/94 E08177 Aspartokinase Sato, Y. et al. “Genetic DNA capable of coding Aspartokinase released from feedback inhibition and its utilization,” Patent: JP 1994261766-A 1 09/20/94 E08178, Feedback inhibition-released Sato, Y. et al. “Genetic DNA capable of coding Aspartokinase released from E08179, Aspartokinase feedback inhibition and its utilization,” Patent: JP 1994261766-A 1 09/20/94 E08180, E08181, E08182 E08232 Acetohydroxy-acid isomeroreductase Inui, M. et al. “Gene DNA coding acetohydroxy acid isomeroreductase,” Patent: JP 1994277067-A 1 10/04/94 E08234 secE Asai, Y. et al. “Gene DNA coding for translocation machinery of protein,” Patent: JP 1994277073-A 1 10/04/94 E08643 FT aminotransferase and Hatakeyama, K. et al. “DNA frament having promoter function in desthiobiotin synthetase promoter coryneform bacterium,” Patent: JP 1995031476-A 1 02/03/95 region E08646 Biotin synthetase Hatakeyama, K. et al. “DNA fragment having promoter function in coryneform bacterium,” Patent: JP 1995031476-A 1 02/03/95 E08649 Aspartase Kohama, K. et al “DNA fragment having promoter function in coryneform bacterium,” Patent: JP 1995031478-A 1 02/03/95 E08900 Dihydrodipicolinate reductase Madori, M. et al. “DNA fragment containing gene coding Dihydro- dipicolinate acid reductase and utilization thereof,” Patent: JP 1995075578-A 1 03/20/95 E08901 Diaminopimelic acid decarboxylase Madori, M. et al. “DNA fragment containing gene coding Diaminopimelic acid decarboxylase and utilization thereof,” Patent: JP 1995075579- A 1 03/20/95 E12594 Serine hydroxymethyltransferase Hatakeyama, K. et al. “Production of L-trypophan,” Patent: JP 1997028391- A 1 02/04/97 E12760, transposase Moriya, M. et al. “Amplification of gene using artificial transposon,” Patent: E12759, JP 1997070291-A 03/18/97 E12758 E12764 Arginyl-tRNA synthetase; diamino- Moriya, M. et al. “Amplification of gene using artificial transposon,” Patent: pimelic acid decarboxylase JP 1997070291-A 03/18/97 E12767 Dihydrodipicolinic acid synthetase Moriya, M. et al. “Amplification of gene using artificial transposon,” Patent: JP 1997070291-A 03/18/97 E12770 aspartokinase Moriya, M. et al. “Amplification of gene using artificial transposon,” Patent: JP 1997070291-A 03/18/97 E12773 Dihydrodipicolinic acid reductase Moriya, M. et al. “Amplification of gene using artificial transposon,” Patent: JP 1997070291-A 03/18/97 E13655 Glucose-6-phosphate dehydrogenase Hatakeyama, K. et al. “Glucose-6-phosphate dehydrogenase and DNA capable of coding the same,” Patent: JP 1997224661-A 1 09/02/97 L01508 IlvA Threonine dehydratase Moeckel, B. et al. “Functional and structural analysis of the threonine dehydratase of Corynebacterium glutamicum,” J. Bacteriol., 174:8065-8072 (1992) L07603 EC 4.2.1.15 3-deoxy-D-arabinoheptulosonate-7- Chen, C. et al. “The cloning and nucleotide sequence of Corynebacterium phosphate synthase glutamicum 3-deoxy-D-arabinoheptulosonate-7-phosphate synthase gene,” FEMS Microbiol. Lett., 107:223-230 (1993) L09232 IlvB; ilvN; ilvC Acetohydroxy acid synthase large Keilhauer, C. et al. “Isoleucine synthesis in Corynebacterium glutamicum: subunit; Acetohydroxy acid synthase molecular analysis of the ilvB-ilvN-ilvC operon,” J. Bacteriol., 175(17): small subunit; Acetohydroxy acid 5595-5603 (1993) isomeroreductase L18874 PtsM Phosphoenolpyruvate sugar Fouet, A et al. “Bacillus subtilis sucrose-specific enzyme II of the phosphotransferase phosphotransferase system: expression in Escherichia coli and homology to enzymes II from enteric bacteria,” PNAS USA, 84(24): 8773-8777 (1987); Lee, J. K. et al. “Nucleotide sequence of the gene encoding the Corynebacterium glutamicum mannose enzyme II and analyses of the deduced protein sequence,” FEMS Microbiol. Lett., 119(1-2): 137-145 (1994) L27123 aceB Malate synthase Lee, H-S. et al. “Molecular characterization of aceB, a gene encoding malate synthase in Corynebacterium glutamicum,” J. Microbiol. Biotechnol., 4(4): 256-263 (1994) L27126 Pyruvate kinase Jetten, M. S. et al. “Structural and funtional analysis of pyruvate kinase from Corynebacterium glutamicum,” Appl. Environ. Microbiol., 60(7): 2501-2507 (1994) L28760 aceA Isocitrate lyase L35906 dtxr Diphtheria toxin repressor Oguiza, J. A. et al. “Molecular cloning, DNA sequence analysis, and characterization of the Corynebacterium diphtheriae dtxR from Brevibacterium lactofermentum,” J. Bacteriol., 177(2): 465-467 (1995) M13774 Prephenate dehydratase Follettie, M. T. et al. “Molecular cloning and nucleotide sequence of the Corynebacterium glutamicum pheA gene,” J. Bacteriol., 167: 695-702 (1986) M16175 5S rRNA Park, Y-H. et al. “Phylogenetic analysis of the coryneform bacteria by 56 rRNA sequences,” J. Bacteriol., 169: 1801-1806 (1987) M16663 trpE Anthranilate synthase, 5′ end Sano, K. et al. “Structure and function of the trp operon control regions of Brevibacterium lactofermentum, a glutamic-acid-producing bacterium,” Gene, 52:191-200 (1987) M16664 trpA Tryptophan synthase, 3′ end Sano, K. et al. “Structure and function of the trp operon control regions of Brevibacterium lactofermentum, a glutamic-acid-producing bacterium,” Gene, 52: 191-200 (1987) M25819 Phosphoenolpyruvate carboxylase O'Regan, M. et al. “Cloning and nucleotide sequence of the Phosphoenolpyruvate carboxylase-coding gene of Corynebacterium glutamicum ATCC 13032,” Gene, 77(2): 237-251 (1989) M85106 23S rRNA gene insertion sequence Roller, C. et al. “Gram-positive bacteria with a high DNA G+C content are characterized by a common insertion within their 23S rRNA genes,” J. Gen. Microbiol., 138: 1167-1175 (1992) M85107, 23S rRNA gene insertion sequence Roller, C. et al. “Gram-positive bacteria with a high DNA G+C content are M85108 characterized by a common insertion within their 23S rRnA genes,” J. Gen. Microbiol., 138: 1167-1175 (1992) M89931 aecD; brnQ; Beta C-S lyase; branched-chain Rossol, I. et al. “The Corynebacterium glutamicum aecD gene encodes a C-S yhbw amino acid uptake carrier; lyase with alpha, beta-elimination activity that degrades aminoethylcysteine,” hypothetical protein yhbw J. Bacteriol., 174(9): 2968-2977 (1992); Tauch, A. et al. “Isoleucine uptake in Corynebacterium glutamicum ATCC 13032 is directed by the brnQ gene product,” Arch. Microbiol., 169(4): 303-312 (1998) S59299 trp Leader gene (promoter) Herry, D. M. et al. “Cloning of the trp gene cluster form a tryptophan- hyperproducing strain of Corynebacterium glutamicum: identification of a mutation in the trp leader sequence,” Appl. Environ. Microbiol., 59(3): 791-799 (1993) U11545 trpD Anthranilate phosphoribosyl- O'Gara, J. P. and Dunican, L. K. (1994) Complete nucleotide sequence of transferase the Corynebacterium glutamicum ATCC 21850 tpD gene.” Thesis, Microbiology Department, University College, Galway, Ireland. U13922 cglIM; cglIR; Putative type II 5-cytosoine Schafer, A. et al. ”Cloning and characterization of a DNA region encoding a clgIIR methyltransferase; putative type II stress-sensitive restriction system from Corynebacterium glutamicum ATCC restriction endonuclease; putative 13032 and analysis of its role in intergeneric conjugation with Escherichia type I or type III restriction coli,” J. Bacteriol., 176(23): 7309-7319 (1994); Schafer, A. et al. “The endonuclease Corynebacterium glutamicum cglIM gene encoding a 5-cytosine in an McrBC-deficient Escherichia coli strain,” Gene, 203(2): 95-101 (1997) U14965 recA U31224 ppx Ankri, S. et al. “Mutations in the Corynebacterium glutamicum proline biosynthetic pathway: A natural bypass of the proA step,” J. Bacteriol., 178(15): 4412-4419 (1996) U31225 proC L-proline: NADP+ 5-oxidoreductase Ankri, S. et al. “Mutations in the Corynebacterium glutamicum proline biosynthetic pathway: A natural bypass of the proA step,” J. Bacteriol., 178(15): 4412-4419 (1996) U31230 obg; proB; unkdh ?; gamma glutamyl kinase; similar to Ankri, S. et al. “Mutations in the Corynebacterium glutamicum proline D-isomer specific 2-hydroxyacid biosynthetic pathway: A natural bypass of the proA step,” J. Bacteriol., dehydrogenases 178(15): 4412-4419 (1996) U31281 bioB Biotin synthase Serebriiskii, I. G., “Two new members of the bio B superfamily: Cloning sequencing and expression of Bio B genes of Methylobacillus flagellatum and Corynebacterium glutamicum,” Gene, 175: 15-22 (1996) U35023 thtR; accBC Thiosulfate sulfurtransferase; acyl Jager, W. et al. “A Corynebacterium glutamicum gene encoding a two- CoA carboxylase domain protein similar to biotin carboylases and biotin-carboxyl-carrier proteins,” Arch. Microbiol., 166(2): 76-82 (1996) U43535 cmr Multidrug resistance protein Jager, W. et al. “A Corynebacterium glutamicum gene conferring multidrug resistance in the heterologous host Escherichia coli,” J. Bacteriol., 179(7): 2449-2451 (1997) U43536 clpB Heat shock ATP-binding protein U53587 aphA-3 3′5″-aminoglycoside phospho- transferase U89648 Corynebacterium glutamicum unidentified sequence involved in histidine biosynthesis, partial sequence X04960 trpA; trpB; trpC; Tryptophan operon Matsui, K. et al. “Complete nucleotide and deduced amino acid sequences of trpD; trpE; trpG the Brevibacterium lactofermentum tryptophan operon,” Nucleic Acids Res., trpL 14(24): 10113-10114 (1986) X07563 lys A DAP decarboxylase (meso-diamino- Yeh, P. et al. “Nucleic sequence of the lysA gene of Corynebacterium pimelate decarboxylase, EC 4.1.1.20 glutamicum and possible mechanisms for modulation of its expression,” Mol. Gen. Genet., 212(1): 112-119 (1988) X14234 EC 4.1.1.31 Phosphoenolpyruvate carboxylase Eikmanns, B. J. et al. “The Phosphoenolpyruvate carboxylase gene of Corynebacterium glutamicum: Molecular cloning, nucleotide sequence, and expression,” Mol. Gen. Genet., 218(2): 330-339 (1989); Lepiniec, L. et al. “Sorghum Phosphoenolpyruvate carboxylase gene family: structure, function and molecular evolution,” Plant. Mol. Biol., 21(3): 487-502 (1993) X17313 fda Fructose-bisphosphate aldolase Von der Osten, C. H. et al. “Molecular cloning, nucleotide sequence and fine-structural analysis of the Corynebacterium glutamicum fda gene: structural comparison of C. glutamicum fructose-1,6-biphosphate aldolase to class I and class II aldolases,” Mol. Microbiol., X53993 dapA L-2, 3-dihydrodipicolinate synthetase Bonnassie, S. et al. “Nucleic sequence of the dapA gene from (EC 4.2.1.52) Corynebacterium glutamicum,” Nucleic Acids Res., 18(21): 6421 (1990) X54223 AttB-related site Cianciotto, N. et al. “DNA sequence homology between att B-related sites of Corynebacterium diphtheria, Corynebacterium ulcerans, Corynebacterium glutamicum, and the attP site of lambdacorynephage,” FEMS. Microbiol, Lett., 66: 299-302 (1990) X54740 argS; lysA Arginyl-tRNA synthetase; Diamino- Marcel, T. et al. “Nucleotide sequence and organization of the upstream pimelate decarboxylase region of the Corynebacterium glutamicum lysA gene,” Mol. Microbiol., 4(11): 1819-1830 (1990) X55994 trpL; trpE Putative leader peptide; anthranilate Heery, D. M. et al. “Nucleotide sequence of the Corynebacterium synthase component 1 glutamicum trpE gene,” Nucleic Acids Res., 18(23): 7138 (1990) X56037 thrC Threonine synthase Han, K. S. et al. “The molecular structure of the Corynebacterium glutamicum threonine synthase gene,” Mol. Microbiol., 4(10): 1693-1702 (1990) X56075 attB-related site Attachment site Cianciotto, N. et al. “DNA sequence homology between att B-related sites of Corynebacterium diphtheriae, Corynebacterium ulcerans, Corynebacterium glutamicum, and the attP site of lambdacorynephage,” FEMS, Microbiol, Lett., 66: 299-302 (1990) X57226 lysC-alpha; Aspartokinase-alpha subunit; Kalinowski, J. et al. “Genetic and biochemical analysis of the Aspartokinase lysC-beta asd Aspartokinase-beta subunit; aspartate from Corynebacterium glutamicum,” Mil. Microbiol., 5(5): beta semialdehyde dehydrogenase 1197-1204 (1991); Kalinowski, J. et al. “Aspartokinase genes lysC alpha and lysC beta overlap and are adjacent to the aspertate beta-semialdehyde dehdrogenase gene asd in Corynebacterium glutamicum,” Mol. Gen. Gene., 224(3): 317-324 (1990) X59403 gap; pgk; tpi Glyceraldehyde-3-phosphate; Eikmanns, B. J. “Identification sequence analysis, and expression of a phosphoglycerate kinase; triose- Corynebacterium glutamicum gene cluster encoding the three glycolytic phosphate isomerase enzymes glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase, and triosephosphate isomeras,” J. Bacteriol., 174(19): 6076-6086 (1992) X59404 gdh Glutamate dehydrogenase Bormann, E. R. et al. “Molecular anylysis of the Corynebacterium glutamicum gdh gene encoding glutamate dehydrogenase,” Mol. Microbiol., 6(3): 317-326 (1992) X60312 lysI L-lysine permease Seep-Feldhaus, A. H. et al. “Molecular analysis of the Corynebacterium glutamicum lysI gene involved in lysine uptake,” Mol. Microbiol., 5(12): 2995-3005 (1991) X66078 cop1 Ps1 protein Joliff, G. et al. “Cloning and nucloetide sequence of the csp1 gene encoding PS1, one of the two major secreted proteins of Corynebacterium glutamicum: The deduced N-terminal region of PS1 is similar to the Mycobacterium antigen 85 complex,” Mol. Microbiol., 6(16): 2349-2362 (1992) X66112 glt Citrate synthase Eikmanns, B. J. et al. “Cloning sequence, expression and transcriptional analysis of the Corynebacterium glutamicum gltA gene encoding citrate synthase,” Microbiol., 140: 1817-1828 (1994) X67737 dapB Dihydrodipicolinate reductase X69103 csp2 Surface layer protein PS2 Peyret, J. L. et al. “Characterization of the cspB gene encoding PS2, an ordered surface-layer protein in Corynebacterium glutamicum,” Mol. Microbiol., 9(1): 97-109 (1993) X69104 IS3 related insertion element Bonamy, C. et al. “Identification of IS1206, a Corynebacterium glutamicum IS3-related insertion sequence and phylogenetic analysis,” Mol. Microbiol., 14(3): 571-581 (1994) X70959 leuA Isopropylmalate synthase Patek, M. et al. “Leucine synthesis in Corynebacterium glutamicum: enzyme activities, structure of leuA, and effect of leuA inactivation on lysine synthesis,” Appl. Environ. Microbiol., 60(1): 133-140 (1994) X71489 icd Isocitrate dehydrogenase (NADP+) Eikmanns, B. J. et al. “Cloning sequence analysis, expression, and inactivation of the Corynebacterium glutamicum icd gene encoding isocitrate dehydrogenase and biochemical characterization of the enzyme,” J. Bacteriol, 177(3): 774-782 (1995) X72855 GDHA Glutamate dehydrogenase (NADP+) X75083, mtrA 5-methyltryptophan resistance Heery, D. M. et al. “A sequence from a tryptophan-hyperproducing strain of X70584 Corynebacterium glutamicum encoding resistance to 5-methyltryptophan,” Biochem. Biophys. Res. Commun, 201(3): 1255-1262 (1994) X75085 recA Fitzpatrick, R. et al. “Construction and characterization of recA mutant strains of Corynebacterium glutamicum and Brevibacterium lactogermentum,” Appl. Microbiol. Biotechnol., 42(4): 575-580 (1994) X75504 aceA; thiX Partial Isocitrate lyase; ? Reinscheid, D. J. et al. “Characterization of the isocitrate lyase gene from Corynebacterium glutamicum and biochemical analysis of the enzyme,” J. Bacteriol., 176(12): 3474-3483 (1994) X76875 ATPase beta-subunit Ludwig, W. et al. “Phylogenetic relationships of bacteria based on comparative sequence analysis of elongation factor Tu and ATP-synthase beta-subunit X77034 tuf Elongation factor Tu Ludwig, W. et at. “Phylogenetic relationships of bacteria based on comparative sequence analysis of elongation factor Tu and ATP-synthase beta-subunit genes,” Antonie Van Leeuwenhoek, 64: 285-305 (1993) X77384 recA Billman-Jacobe, H. “Nucleotide sequence of a recA gene from Corynebacterium glutamicum,” DNA seq., 4(6): 403-404 (1994) X78491 aceB Malate synthase Reinscheid, D. J. et al. “Malate synthase from Corynebacterium glutamicum pta-ack operon encoding phosphotransacetylase: sequence analysis,” Microbiology, 140: 3099-3108 (1994) X80629 16S rDNA 16S ribosomal RNA Rainey, F. A. et al. “Phylogenetic analysis of the genera Rhodococcus and Norcardia and evidence for the evolutionary origin of the genus Norcadia from within the radiation of Rhodococcus species,” Mircrobiol., 141: 523-528 (1995) X81191 gluA; gluB; gluC; Glutamate uptake system Kronemeyer, W. et al. “Structure of the gluABCD cluster encoding the gluD glutamate uptake system of Corynebacterium glutamicum,” J. Bacteriol., 177(5): 1152-1158 (1995) X81379 dapE Succinyldiaminopimelate Wehrmann, A. et al. “Analysis of different DNA fragments of desuccinylase Corynebacterium glutamicum complementing dapE of Escherichia coli,” Microbiology, 40: 3349-56 (1994) X82061 16S rDNA 16S ribosomal RNA Ruimy, R. et at. “Phylogeny of the genus Corynebacterium deduced from analyses of small-subunit ribosomal DNA sequences,” Int. J. Syst. Bacteriol., 45(4): 740-746 (1995) X82928 asd; lysC Aspartate-semialdehyde Serebrijski, I. et al. “Multicopy suppression by asd gene and osmotic stress- dehydrogenase; ? dependent complementation by heterologous proA in proA mutants,” J. Bacteriol., 177(24): 7255-7260 (1995) X82929 proA Gamma-glutamyl phosphate Serebrijski, I. et al. “Multicopy suppression by asd gene and osmotic stress- reductase dependent complementation by heterologous proA in proA mutants,” J. Bacteriol., 177(24): 7255-7260 (1995) X84257 16S rDNA 16S ribosomal RNA Pascual, C. et al. “Phylogenetic analysis of the genus Corynebacterium based on 16S rRNA gene sequences,” Int. J. Syst. Bacteriol., 45(4): 724-728(1995) X85965 aroP; dapE Aromatic amino acid permease; ? Wehrmann et al. “Functional analysis of sequences adjacent to dapE of C. glutamicum proline reveals the presence of aroP, which encodes the aromatic amino acid transporter,” J. Bacteriol., 177(20): 5991-5993 (1995) X86157 argB; argC; argD; Acetylglutamate kinase; N-acetyl- Sakanyan, V. et al. “Genes and enzymes of the acetyl cycle of arginine argF; argJ gamma-glutamyl-phosphate biosynthesis in Corynebacterium glutamicum: enzyme evolution in the early reductase; acetylornithine amino- steps of the arginine pathway, Microbilogy, 142: 99-108 (1996) transferase; ornithine carbamoyl- transferase; glutamate N- acetyltransferase X89084 pta; ackA Phosphate acetyltransferase; acetate Reinscheid, D. J. et al. “Cloning, sequence analysis, expression and kinase inactivation of the Corynebacterium glutamicum pta-ack operon encoding phosphotransacetylase and acetate kinase,” Microbiology, 145: 503-513 (1999) X89850 attB Attachment site Le Marrec, C. et al. “Genetic characterization of site-specific integration functions of phi AAU2 infecting “Arthrobacter aureus C70” J. Bacteriol., 178(7): 1996-2004 (1996) X90356 Promoter fragment F1 Patek, M. et al. “Promoters from Corynebacterium glutamicum: cloning, molecular analysis and search for a consensus motif,” Microbiology, 142: 1297-1309 (1996) X90357 Promoter fragment F2 Patek, M. et al. “Promoters from Corynebacterium glutamicum: cloning, molecular analysis and search for a consensus motif,” Microbiology, 142: 1297-1309 (1996) X90358 Promoter fragment F10 Patek, M. et al. “Promoters from Corynebacterium glutamicum: cloning, molecular analysis and search for a consensus motif,” Microbiology, 142: 1297-1309 (1996) X90359 Promoter fragment F13 Patek, M. et al. “Promoters from Corynebacterium glutamicum: cloning, molecular analysis and search for a consensus motif,” Microbiology, 142: 1297-1309 (1996) X90360 Promoter fragment F22 Patek, M. et al. “Promoters from Corynebacterium glutamicum: cloning, molecular analysis and search for a consensus motif,” Microbiology, 142: 1297-1309 (1996) X90361 Promoter fragment F34 Patek, M. et al. “Promoters from Corynebacterium glutamicum: cloning, molecular analysis and search for a consensus motif,” Microbiology, 142: 1297-1309 (1996) X90362 Promoter fragment F37 Patek, M. et al. “Promoters from C. glutamicum: cloning, molecular analysis and search for a consensus motif,” Microbiology,” 142: 1297-1309 (1996) X90363 Promoter fragment F45 Patek, M. et al. “Promoters from Corynebacterium glutamicum: cloning, molecular analysis and search for a consensus motif,” Microbiology, 142: 1297-1309 (1996) X90364 Promoter fragment F64 Patek, M. et al. “Promoters from Corynebacterium glutamicum: cloning, molecular analysis and search for a consensus motif,” Microbiology, 142: 1297-1309 (1996) X90365 Promoter fragment F75 Patek, M. et al. “Promoters from Corynebacterium glutamicum: cloning, molecular analysis and search for a consensus motif,” Microbiology, 142: 1297-1309 (1996) X90366 Promoter fragment PF101 Patek, M. et al. “Promoters from Corynebacterium glutamicum: cloning, molecular analysis and search for a consensus motif,” Microbiology, 142: 1297-1309 (1996) X90367 Promoter fragment PF104 Patek, M. et al. “Promoters from Corynebacterium glutamicum: cloning, molecular analysis and search for a consensus motif,” Microbiology, 142: 1297-1309 (1996) X90368 Promoter fragment PF109 Patek, M. et al. “Promoters from Corynebacterium glutamicum: cloning, molecular analysis and search for a consensus motif,” Microbiology, 142: 1297-1309 (1996) X93513 amt Ammonium transport system Siewe, R. M. et al. “Functional and genetic characterization of the (methyl) ammonium uptake carrier of Corynebacterium glutamicum, ” J. Biol. Chem., 271(10): 5398-5403 (1994) X93514 betP Glycine betaine transport system Peter, H. et al. “Isolation, characterization, and expression of the Corynebacterium glutamicum betP gene, encoding the transport system for the compatible solute glycin betaine,” J. Bacteriol., 178(17): 5229-5234 (1996) X95649 orf4 Patek, M. et al. “Identification and transcriptional analysis of the dapB- ORF2-dapA-ORF4 operon of Corynebacterium glutamicum, encoding two enzymes involved in L-lysine synthesis,” Biotechnol. Lett., 19: 1113- 1117 (1997) X96471 lysE; lysG Lysine exporter protein; Lysine Vrljic, M. et al. “A new type of transpoter with a new type of cellular export regulator protein function: L-lysine export from Corynebacterium glutamicum,” Mol. Microbiol., 22(5): 815-826 (1996) X96580 panB; panC; xylB 3-methyl-2-oxobutanoate Sahm, H. et al. “D-pantothenate synthesis in Corynebacterium glutamicum hydroxymethyltransferase; pantoate- and use of panBC and genes encoding L-valine synthesis for D-pantothenate beta- X96962 Insertion sequence IS1207 and transposase X99289 Elongation factor P Ramos, A. et al. “Cloning, sequencing and expression of the gene encoding elongation factor P in the amino-acid producer Brevibacterium lactofermentum (Corynebacterium glutamicum ATCC 13869),” Gene, 198: 217-222 (1997) Y00140 thrB Homoserine kinase Mateos, L. M. et al. “Nucleotide sequence of the homoserine kinase (thrB) gene of the Brevibacterium lactofermentum,” Nucleic Acids Res., 15(9): 3922 (1987) Y00151 ddh Meso-diaminopimelate D- Ishino, S. et al. “Nucleotide sequence of the meso-diaminopimelate D- dehydrogenase (EC 1.4.1.16) dehydrogenase gene from Corynebacterium glutamicum,” Nucleic Acids Res., 15(9): 3917 (1987) Y00476 thrA Homoserine dehydrogenase Mateos, L. M. et al. “Nucleotide sequence of the homoserine dehydrogenase (thrA) gene of the Brevibacterium lactofermentum,” Nucleic Acids Res., 15(24): 10598 (1987) Y00546 hom; thrB Homoserine dehydrogenase; Peoples, O. P. et al. “Nucleotide sequence and fine structural analysis of the homoserine kinase Corynebacterium glutamicum hom-thrB operon,” Mol. Microbiol., 2(1): 63-72 (1988) Y08964 murC; ftsQ/divD; UPD-N-acetylmuramate-alanine Honrubia, M. P. et al. “Identification, characterization, and chromosomal ftsZ ligase; division initiation protein or organization of the ftsZ gene from Brevibacterium lactofermentum,” Mol. cell division protein; cell Gen. Genet., 259(1): 97-104 (1998) division protein Y09163 putP High affinity proline transport system Peter, H. et al. Isolation of the putP gene of Corynebacterium glutamicum proline and characterization of a low-affinity uptake system for compatible solutes,” Arch. Microbiol., 168(2): 143-151 (1997) Y09548 pyc Pyruvate carboxylase Peters-Wendisch, P. G. et al. “Pyruvate caroxylase from Corynebacterium glutamicum: characterization, expression and inactivation of the pyc gene,” Microbiology, 144: 915-927 (1998) Y09578 leuB 3-isopropylmalate dehydrogenase Patek, M. et al. “Analysis of leuB ene from Corynebacterium glutamicum,” Appl. Microbiol. Biotechnol., 50(1): 42-47 (1998) Y12472 Attachment site bacteriophage Phi-16 Moreau, S. et al. “Site-specific integration of corynephage Phi-16: The construction of an integration vector,” Microbiol., 145: 539-548 (1999) Y12537 proP Proline/ectoine uptake system protein Peter, H. et al. “Corynebacterium glutamicum is equipped with four secondary carriers for compatible solutes: Identification, sequencing, and characterization of the proline/ectoine uptake system, ProP, and the ectoine/ proline/glycine betaine carrier, EctP,” J. Bacteriol., 180(22): 6005-6012 (1998) Y13221 glnA Glutamine synthetase I Jakoby, M. et al. “Isolation of Corynebacterium glutamicum glnA gene encoding glutamine synthetase I,” FEMS Microbiol. Lett., 154(1): 81-88 (1997) Y16642 lpd Dihydrolipoamide dehydrogenase Y18059 Attachment site Corynephage 304L Moreau, S. et al. “Analysis of the integration funtions of &phi; 304L: An integrase module among corynephages,” Virology, 255(1): 150-159 (1999) Y21501 argS; lysA Arginyl-tRNA synthetase; diamino- Oguiza, J. A. et al. “A gene encoding arginyl-tRNA synthetase is located in pimelate decarboxylase (partial) the upstream region of the lysA gene in Brevibacterium lactofermentum: Regulation of argS-lysA cluster expression by arginine,” J. Bacteriol., 175(22): 7356-7362 (1993) Y21502 dapA; dapB Dihydrodipicolinate synthase; Pisabarro, A. et al. “A cluster of three genes (dapA, orf2, and dapB) of dihydrodipicolinate reductase Brevibacterium lactofermentum encodes dihydrodipicolinate reductase, and a third polypeptide of unknown function,” J. Bacteriol., 175(9): 2743-2749 (1993) Z29563 thrC Threonine synthase Malumbres, M. et al. “Analysis and expression of the thrC gene of the encoded threonine synthase,” Appl. Environ. Microbiol., 60(7)2209-2219 (1994) Z46753 16S rDNA Gene for 16S ribosomal RNA Z49822 sigA SigA sigma factor Oguiza, J. A. et al “Multiple sigma factor genes in Brevibacterium lactofermentum: Characterization of sigA and sigB,” J. Bacteriol., 178(2): 550-553 (1996) Z49823 galE; dtxR Catalytic activity UDP-galactose 4- Oguiza, J. A. et al “The galE gene encoding the UDP-galactose 4-epimerase epimerase; diphtheria toxin regulatory of Brevibacterium lactofermentum is coupled transcriptionally to the dmdR protein gene,” Gene, 177: 103-107 (1996) Z49824 orf1; sigB ?; SigB sigma factor Oguiza, J. A. et al “Multiple sigma factor genes in Brevibacterium lactofermentum: Characterization of sigA and sigB,” J. Bacteriol., 178(2): 550-553 (1996) Z66534 Transposase Correia, A. et al. “Cloning and characterization of an IS-like element present in the genome of Brevibacterium lactofermentum ATCC 13869,” Gene, 170(1): 91-94 (1996)

[0228] TABLE 3 Corynebacterium and Brevibacterium Strains Which May be Used in the Practice of the Invention Other Genus species ATCC FERM NRRL CECT NCIMB CBS NCTC DSMZ origin Brevibacterium ammoniagenes 21054 Brevibacterium ammoniagenes 19350 Brevibacterium ammoniagenes 19351 Brevibacterium ammoniagenes 19352 Brevibacterium ammoniagenes 19353 Brevibacterium ammoniagenes 19354 Brevibacterium ammoniagenes 19355 Brevibacterium ammoniagenes 19356 Brevibacterium ammoniagenes 21055 Brevibacterium ammoniagenes 21077 Brevibacterium ammoniagenes 21553 Brevibacterium ammoniagenes 21580 Brevibacterium ammoniagenes 39101 Brevibacterium butanicum 21196 Brevibacterium divaricatum 21792 P928 Brevibacterium flavum 21474 Brevibacterium flavum 21129 Brevibacterium flavum 21518 Brevibacterium flavum B11474 Brevibacterium flavum B11472 Brevibacterium flavum 21127 Brevibacterium flavum 21128 Brevibacterium flavum 21427 Brevibacterium flavum 21475 Brevibacterium flavum 21517 Brevibacterium flavum 21528 Brevibacterium flavum 21529 Brevibacterium flavum B11477 Brevibacterium flavum B11478 Brevibacterium flavum 21127 Brevibacterium flavum B11474 Brevibacterium healii 15527 Brevibacterium ketoglutamicum 21004 Brevibacterium ketoglutamicum 21089 Brevibacterium ketosoreductum 21914 Brevibacterium lactofermentum 70 Brevibacterium lactofermentum 74 Brevibacterium lactofermentum 77 Brevibacterium lactofermentum 21798 Brevibacterium lactofermentuin 21799 Brevibacterium lactofermentum 21800 Brevibacterium lactofermentum 21801 Brevibacterium lactofermentum B11470 Brevibacterium lactofermentum B11471 Brevibacterium lactofermentum 21086 Brevibacterium lactofermentum 21420 Brevibacterium lactofermentum 21086 Brevibacterium lactofermentum 31269 Brevibacterium linens 9174 Brevibacterium linens 19391 Brevibacterium linens 8377 Brevibacterium paraffinolyticum 11160 Brevibacterium spec. 717.73 Brevibacterium spec. 717.73 Brevibacterium spec. 14604 Brevibacterium spec. 21860 Brevibacterium spec. 21864 Brevibacterium spec. 21865 Brevibacterium spec. 21866 Brevibacterium spec. 19240 Corynebacterium acetoacidophilum 21476 Corynebacterium acetoacidophilum 13870 Corynebacterium acetoglutamicum B11473 Corynebacterium acetoglutamicum B11475 Corynebacterium acetoglutamicum 15806 Corynebacterium acetoglutamicum 21491 Corynebacterium acetoglutamicum 31270 Corynebacterium acetophilum B3671 Corynebacterium ammoniagenes 6872 2399 Corynebacterium ammoniagenes 15511 Corynebacterium fujiokense 21496 Corynebacterium glutamicum 14067 Corynebacterium glutamicum 39137 Corynebacterium glutamicum 21254 Corynebacterium glutamicum 21255 Corynebacterium glutamicum 31830 Corynebacterium glutamicum 13032 Corynebacterium glutamicum 14305 Corynebacterium glutamicum 15455 Corynebacterium glutamicum 13058 Corynebacterium glutamicum 13059 Corynebacterium glutamicum 13060 Corynebacterium glutamicum 21492 Corynebacterium glutamicum 21513 Corynebacterium glutamicum 21526 Corynebacterium glutamicum 21543 Corynebacterium glutamicum 13287 Corynebacterium glutamicum 21851 Corynebacterium glutamicum 21253 Corynebacterium glutamicum 21514 Corynebacterium glutamicum 21516 Corynebacterium glutamicum 21299 Corynebacterium glutamicum 21300 Corynebacterium glutamicum 39684 Corynebacterium glutamicum 21488 Corynebacterium glutamicum 21649 Corynebacterium glutamicum 21650 Corynebacterium glutamicum 19223 Corynebacterium glutamicum 13869 Corynebacterium glutamicum 21157 Corynebacterium glutamicum 21158 Corynebacterium glutamicum 21159 Corynebacterium glutamicum 21355 Corynebacterium glutamicum 31808 Corynebacterium glutamicum 21674 Corynebacterium glutamicum 21562 Corynebacterium glutamicum 21563 Corynebacterium glutamicum 21564 Corynebacterium glutamicum 21565 Corynebacterium glutamicum 21566 Corynebacterium glutamicum 21567 Corynebacterium glutamicum 21568 Corynebacterium glutamicum 21569 Corynebacterium glutamicum 21570 Corynebacterium glutamicum 21571 Corynebacterium glutamicum 21572 Corynebacterium glutamicum 21573 Corynebacterium glutamicum 21579 Corynebacterium glutamicum 19049 Corynebacterium glutamicum 19050 Corynebacterium glutamicum 19051 Corynebacterium glutamicum 19052 Corynebacterium glutamicum 19053 Corynebacterium glutamicum 19054 Corynebacterium glutamicum 19055 Corynebacterium glutamicum 19056 Corynebacterium glutamicum 19057 Corynebacterium glutamicum 19058 Corynebacterium glutamicum 19059 Corynebacterium glutamicum 19060 Corynebacterium glutamicum 19185 Corynebacterium glutamicum 13286 Corynebacterium glutamicum 21515 Corynebacterium glutamicum 21527 Corynebacterium glutamicum 21544 Corynebacterium glutamicum 21492 Corynebacterium glutamicum B8183 Corynebacterium glutamicum B8182 Corynebacterium glutamicum B12416 Corynebacterium glutamicum B12417 Corynebacterium glutamicum B12418 Corynebacterium glutamicum B11476 Corynebacterium glutamicum 21608 Corynebacterium lilium P973 Corynebacterium nitrilophilus 21419 11594 Corynebacterium spec. P4445 Corynebacterium spec. P4446 Corynebacterium spec. 31088 Corynebacterium spec. 31089 Corynebacterium spec. 31090 Corynebacterium spec. 31090 Corynebacterium spec. 31090 Corynebacterium spec. 15954 20145 Corynebacterium spec. 21857 Corynebacterium spec. 21862 Corynebacterium spec. 21863 Corynebacterium Glutamicum* ASO19 Corynebacterium Glutamicum** ASO19 E12 Corynebacterium Glutamicum*** HL457 Corynebacterium Glutamicum**** HL459

[0229] TABLE 4 ALIGNMENT RESULTS length % homology Date of ID # (NT) Genbank Hit Length Accession Name of Genbank Hit Source of Genbank Hit (GAP) Deposit rxa00657 906 GB_BA1:AF064700 3481 AF064700 Rhodococcus sp NO1-1 CprS and CprR genes, complete cds. Rhodococcus sp 40,265 15-Jul-98 metz 1314 GB_BA2:MTV016 53662 AL021841 Mycobacterium tuberculosis H37Rv complete genome, segment 143/162 Mycobacterium tuberculosis 61,278 23-Jun-99 metc 978 GB_BA2:CORCSLYS 2821 M89931 Corynebacterium glutamicum beta C-S lyase (aecD) and branched-chain amino acid Corynebacterium glutamicum 99,591 04-JUN-1998 upta rxa00023 3579 GB_EST33:AI776129 483 AI776129 EST257217 tomato resistant, Cornell Lycopersicon esculentum cDNA clone Lycopersicon esculentum 40,956 29-Jun-99 cLER17D3, mRNA sequence. GB_EST33:AI776129 483 AI776129 EST257217 tomato resistant, Cornell Lycopersicon esculentum cDNA clone Lycopersicon esculentum 40,956 29-Jun-99 cLER17D3, mRNA sequence. rxa00044 1059 EM_PAT:E11760 6911 E11760 Base sequence of sucrase gene. Corynebacterium glutamicum 42,979 08-OCT-1997 (Rel. 52, Created) GB_PAT:I26124 6911 I26124 Sequence 4 from U.S. Pat. 5556776. Unknown. 42,979 07-OCT-1996 GB_BA2:ECOUW89 176195 U00006 E. coli chromosomal region from 89.2 to 92.8 minutes. Escherichia coli 39,097 17-DEC-1993 rxa00064 1401 GB_PAT:E16763 2517 E16763 gDNA encoding aspartate transferase (AAT). Corynebacterium glutamicum 95,429 28-Jul-99 GB_HTG2:AC007892 134257 AC007892 Drosophila melanogaster chromosome 3 clone BACR02O03 (D797) RPCI-98 Drosophila melanogaster 31,111 2-Aug-99 02.O.3 map 99B-99B strain y; cn bw sp, *** SEQUENCING IN PROGRESS ***, 113 unordered pieces. GB_HTG2:AC007892 134257 AC007892 Drosophila melanogaster chromosome 3 clone BACR02O03 (D797) RPCI-98 Drosophila melanogaster 31,111 2-Aug-99 02.O.3 map 99B-99B strain y; cn bw sp, *** SEQUENCING IN PROGRESS ***, 113 unordered pieces. rxa00072 rxa00105 798 GB_BA1:MTV002 56414 AL008967 Mycobacterium tuberculosis H37Rv complete genome; segment 122/162. Mycobacterium tuberculosis 37,753 17-Jun-98 GB_BA1:ECU29581 71128 U29581 Escherichia coli K-12 genome; approximately 63 to 64 minutes. Escherichia coli 35,669 14-Jan-97 GB_BA2:AE000366 10405 AE000366 Escherichia coli K-12 MG1655 section 256 of 400 of the complete genome. Escherichia coli 35,669 12-Nov-98 rxa00106 579 GB_EST15:AA494237 367 AA494237 ng83f04.s1 NCI_CGAP_Pr6 Homo sapiens cDNA clone IMAGE:941407 Homo sapiens 42,896 20-Aug-97 similar to SW:DYR_LACCA P00381 DIHYDROFOLATE REDUCTASE;, mRNA sequence. GB_BA2:AF161327 2021 AF161327 Corynebacterium diphtheriae histidine kinase ChrS (chrS) and response Corynebacterium diphtheriae 40,210 9-Sep-99 regulator ChrA (chrA) genes, complete cds. GB_PAT:AR041189 654 AR041189 Sequence 4 from U.S. Pat. 5811286. Unknown. 41,176 29-Sep-99 rxa00115 1170 GB_PR4:AC007110 148336 AC007110 Homo sapiens chromosome 17, clone hRPK.472_J_18, complete sequence. Homo sapiens 36,783 30-MAR-1999 GB_HTG3:AC008537 170030 AC008537 Homo sapiens chromosome 19 clone CIT-HSPC_490E21, *** SEQUENCING Homo sapiens 40,296 2-Sep-99 IN PROGRESS ***, 93 unordered pieces. GB_HTG3:AC008537 170030 AC008537 Homo sapiens chromosome 19 clone CIT-HSPC_490E21, *** SEQUENCING Homo sapiens 40,296 2-Sep-99 IN PROGRESS ***, 93 unordered pieces. rxa00116 1284 GB_BA2:AF062345 16458 AF062345 Caulobacter crescentus Sst1 (sst1), S-layer protein subunit (rsaA), ABC Caulobacter crescentus 36,235 19-OCT-1999 transporter (rsaD), membrane forming unit (rsaE), putative GDP-mannose-4,6- dehydratase (IpsA), putative acetyltransferase (IpsB), putative perosamine synthetase (IpsC), putative mannosyltransferase (IpsD), putative mannosyltransferase (IpsE), outer membrane protein (rsaF), and putative perosamine transferase (IpsE) genes, complete cds. GB_PAT:I18647 3300 I18647 Sequence 6 from U.S. Pat. 5500353. Unknown. 36,821 07-OCT-1996 GB_GSS13:AQ446197 751 AQ446197 nbxb0062D16r CUGI Rice BAC Library Oryza sativa genomic clone Oryza sativa 38,124 8-Apr-99 nbxb0062D16r, genomic survey sequence. rxa00131 732 GB_BA1:MTY20B11 36330 Z95121 Mycobacterium tuberculosis H37Rv complete genome; segment 139/162. Mycobacterium tuberculosis 43,571 17-Jun-98 GB_BA1:SAR7932 15176 AJ007932 Streptomyces argillaceus mithramycin biosynthetic genes. Streptomyces argillaceus 41,116 15-Jun-99 GB_BA1:MTY20B11 36330 Z95121 Mycobacterium tuberculosis H37Rv complete genome; segment 139/162. Mycobacterium tuberculosis 39,726 17-Jun-98 rxa00132 1557 GB_BA1:MTY20B11 36330 Z95121 Mycobacterium tuberculosis H37Rv complete genome; segment 139/162. Mycobacterium tuberculosis 36,788 17-Jun-98 GB_IN2:TVU40872 1882 U40872 Trichomonas vaginalis S-adenosyl-L-homocysteine hydrolase gene, complete Trichomonas vaginalis 61,914 31-OCT-1996 cds. GB_HTG6:AC010706 169265 AC010706 Drosophila melanogaster chromosome X clone BACR36D15 (D887) RPCI-98 Drosophila melanogaster 51,325 22-Nov-99 36.D.15 map 13C-13E strain y; cn bw sp, *** SEQUENCING IN PROGRESS ***, 74 unordered pieces. rxa00145 1059 GB_BA1:MTCY2B12 20431 Z81011 Mycobacterium tuberculosis H37Rv complete genome; segment 61/162. Mycobacterium tuberculosis 63,365 18-Jun-98 GB_BA1:PSEPYRBX 2273 L19649 Pseudomonas aeruginosa aspartate transcarbamoylase (pyrB) and Pseudomonas aeruginosa 56,080 26-Jul-93 dihydroorotase-like (pyrX) genes, complete cds's. GB_BA1:LLPYRBDNA 1468 X84262 L. leichmannii pyrB gene. Lactobacillus leichmannii 47,514 29-Apr-97 rxa00146 1464 GB_BA1:MTCY2B12 20431 Z81011 Mycobacterium tuberculosis H37Rv complete genome; segment 61/162. Mycobacterium tuberculosis 60,714 18-Jun-98 GB_BA1:MTCY154 13935 Z98209 Mycobacterium tuberculosis H37Rv complete genome; segment 121/162. Mycobacterium tuberculosis 39,229 17-Jun-98 GB_BA1:MSGY154 40221 AD000002 Mycobacterium tuberculosis sequence from clone y154. Mycobacterium tuberculosis 36,618 03-DEC-1996 rxa00147 1302 GB_BA1:MTCY2B12 20431 Z81011 Mycobacterium tuberculosis H37Rv complete genome; segment 61/162. Mycobacterium tuberculosis 61,527 18-Jun-98 GB_BA1:MSGB937CS 38914 L78820 Mycobacterium leprae cosmid B937 DNA sequence. Mycobacterium leprae 59,538 15-Jun-96 GB_BA1:PAU81259 7285 U81259 Pseudomonas aeruginosa dihydrodipicolinate reductase (dapB) gene, partial Pseudomonas aeruginosa 55,396 23-DEC-1996 cds, carbamoylphosphate synthetase small subunit (carA) and carbamoylphosphate synthetase large subunit (carB) genes, complete cds, and FtsJ homolog (ftsJ) gene, partial cds. rxa00156 1233 GB_BA1:SC9B10 33320 AL009204 Streptomyces coelicolor cosmid 9B10. Streptomyces coelicolor 52,666 10-Feb-99 GB_BA2:AF002133 15437 AF002133 Mycobacterium avium strain GIR10 transcriptional regulator (mav81) gene, Mycobacterium avium 54,191 26-MAR-1998 partial cds, aconitase (acn), invasin 1 (inv1), invasin 2 (inv2), transcriptional regulator (moxR), ketoacyl-reductase (fabG), enoyl-reductase (inhA) and ferrochelatase (mav272) genes, complete cds. GB_BA1:D85417 7984 D85417 Propionibacterium freudenreichii hemY, hemH, hemB, hemX, hemR and hemL Propionibacterium 46,667 6-Feb-99 genes, complete cds. freudenreichii rxa00166 783 GB_HTG3:AC008167 174223 AC008167 Homo sapiens clone NH0172O13, *** SEQUENCING IN PROGRESS ***, 7 Homo sapiens 37,451 21-Aug-99 unordered pieces. GB_HTG3:AC008167 174223 AC008167 Homo sapiens clone NH0172O13, *** SEQUENCING IN PROGRESS ***, 7 Homo sapiens 37,451 21-Aug-99 unordered pieces. GB_HTG4:AC010118 80605 AC010118 Drosophila melanogaster chromosome 3L/62B1 clone RPCI98-10D15, *** Drosophila melanogaster 38,627 16-OCT-1999 SEQUENCING IN PROGRESS ***, 51 unordered pieces. rxa00198 672 GB_BA1:AB024708 8734 AB024708 Corynebacterium glutamicum gltB and gltD genes for glutamine 2-oxoglutarate Corynebacterium glutamicum 92,113 13-Mar-1999 aminotransferase large and small subunits, complete cds. GB_BA1:AB024708 8734 AB024708 Corynebacterium glutamicum gltB and gltD genes for glutamine 2-oxoglutarate Corynebacterium glutamicum 93,702 13-MAR-1999 aminotransferase large and small subunits, complete cds. GB_EST24:AI232702 528 AI232702 EST229390 Normalized rat kidney, Bento Soares Rattus sp, cDNA clone Rattus sp 34,221 31-Jan-99 RKICF35 3′ end, mRNA sequence. rxa00216 1113 GB_HTG2:HSDJ850E9 117353 AL121758 Homo sapiens chromosome 20 clone RP5-850E9, *** SEQUENCING IN Homo sapiens 37,965 03-DEC-1999 PROGRESS ***, in unordered pieces. GB_HTG2:HSDJ850E9 117353 AL121758 Homo sapiens chromosome 20 clone RP5-850E9, *** SEQUENCING IN Homo sapiens 37,965 03-DEC-1999 PROGRESS ***, in unordered pieces. GB_PR2:CNS01DSA 159400 AL121766 Human chromosome 14 DNA sequence *** IN PROGRESS *** BAC R-412H8 Homo sapiens 38,796 11-Nov-99 of RPCI-11 library from chromosome 14 of Homo sapiens (Human), complete sequence. rxa00219 1065 GB_HTG2:AC005079_0 110000 AC005079 Homo sapiens clone RG252P22, *** SEQUENCING IN PROGRESS ***, 3 Homo sapiens 38,227 22-Nov-98 unordered pieces. GB_HTG2:AC005079_1 110000 AC005079 Homo sapiens clone RG252P22, *** SEQUENCING IN PROGRESS ***, 3 Homo sapiens 38,227 22-Nov-98 unordered pieces. GB_HTG2:AC005079_1 110000 AC005079 Homo sapiens clone RG252P22, *** SEQUENCING IN PROGRESS ***, 3 Homo sapiens 38,227 22-Nov-98 unordered pieces. rxa00223 1212 GB_BA1:PPEA3NIF 19771 X99694 Plasmid pEA3 nitrogen fixation genes. Enterobacter agglomerans 48,826 2-Aug-96 GB_BA2:AF128444 2477 AF128444 Rhodobacter capsulatus molybdenum cofactor biosynthetic gene cluster, Rhodobacter capsulatus 40,135 22-MAR-1999 partial sequence. GB_HTG4:AC010111 138938 AC010111 Drosophila melanogaster chromosome 3L/70C1 clone RPCI98-9B18, *** Drosophila melanogaster 39,527 16-OCT-1999 SEQUENCING IN PROGRESS ***, 64 unordered pieces. rxa00229 803 GB_BA2:AF124518 1758 AF124518 Corynebacterium glutamicum 3-dehydroquinase (aroD) and shikimate Corynebacterium glutamicum 98,237 18-MAY-1999 dehydrogenase (aroE) genes, complete cds. GB_PR3:AC004593 150221 AC004593 Homo sapiens PAC clone DJ0964C11 from 7p14-p15, complete sequence. Homo sapiens 36,616 18-Apr-98 GB_HTG2:AC006907 188972 AC006907 Caenorhabditis elegans clone Y76B12, *** SEQUENCING IN PROGRESS ***, Caenorhabditis elegans 37,095 26-Feb-99 25 unordered pieces. rxa00241 1626 GB_BA1:CGLYSI 4232 X60312 C. glutamicum lysl gene for L-lysine permease. Corynebacterium glutamicum 100,000 30-Jan-92 GB_HTG1:PFMAL13P1 192581 AL049180 Plasmodium falciparum chromosome 13 strain 3D7, *** SEQUENCING IN Plasmodium falciparum 34,947 11-Aug-99 PROGRESS ***, in unordered pieces. GB_HTG1:PFMAL13P1 192581 AL049180 Plasmodium falciparum chromosome 13 strain 3D7, *** SEQUENCING IN Plasmodium falciparum 34,947 11-Aug-99 PROGRESS ***, in unordered pieces. rxa00262 1197 GB_IN2:EHU89655 3219 U89655 Entamoeba histolytica unconventional myosin IB mRNA, complete cds. Entamoeba histolytica 36,496 23-MAY-1997 GB_IN2:EHU89655 3219 U89655 Entamoeba histolytica unconventional myosin IB mRNA, complete cds. Entamoeba histolytica 37,544 23-MAY-1997 rxa00266 531 GB_RO:AF016190 2939 AF016190 Mus musculus connexin-36 (Cx36) gene, complete cds. Mus musculus 41,856 9-Feb-99 EM_PAT:E09719 3505 E09719 DNA encoding precursor protein of alkaline cellulase. Bacillus sp. 34,741 08-OCT-1997 (Rel. 52, Created) GB_PAT:E02133 3494 E02133 gDNA encoding alkaline cellulase. Bacillus sp. 34,741 29-Sep-97 rxa00278 1155 GB_IN1:CELK05F6 36912 AF040653 Caenorhabditis elegans cosmid K05F6. Caenorhabditi elegans 36,943 6-Jan-98 GB_BA1:CGU43535 2531 U43535 Corynebacterium glutamicum multidrug resistance protein (cmr) gene, Corynebacterium glutamicum 36,658 9-Apr-97 complete cds. GB_RO:RNU30789 3510 U30789 Rattus norvegicus clone N27 mRNA. Rattus norvegicus 38,190 20-Aug-96 rxa00295 1125 GB_BA2:CGU31281 1614 U31281 Corynebacterium glutamicum biotin synthase (bioB) gene, complete cds. Corynebacterium glutamicum 99,111 21-Nov-96 GB_BA1:BRLBIOBA 1647 D14084 Brevibacterium flavum gene for biotin synthetase, complete cds. Corynebacterium glutamicum 98,489 3-Feb-99 GB_PAT:E03937 1005 E03937 DNA sequence encoding Brevibacterium flavum biotin-synthase. Corynebacterium glutamicum 98,207 29-Sep-97 rxa00323 1461 GB_BA1:MTCY427 38110 Z70692 Mycobacterium tuberculosis H37Rv complete genome; segment 99/162. Mycobacterium tuberculosis 35,615 24-Jun-99 GB_BA1:MSGB32CS 36404 L78818 Mycobacterium leprae cosmid B32 DNA sequence. Mycobacterium leprae 60,917 15-Jun-96 GB_BA1:MTCY427 38110 Z70692 Mycobacterium tuberculosis H37Rv complete genome; segment 99/162. Mycobacterium tuberculosis 44,60 24-Jun-99 rxa00324 3258 GB_BA1:MSGB32CS 36404 L78818 Mycobacterium leprae cosmid B32 DNA sequence. Mycobacterium leprae 52,516 15-Jun-96 GB_BA1:MTCY427 38110 Z70692 Mycobacterium tuberculosis H37Rv complete genome; segment 99/162. Mycobacterium tuberculosis 38,079 24-Jun-99 GB_OM:BOVELA 3242 J02717 Bovine elastin a mRNA, complete cds. Bos taurus 39,351 27-Apr-93 rxa00330 1566 GB_BA1:CGTHRC 3120 X56037 Corynebacterium glutamicum thrC gene for threonine synthase (EC 4.2.99.2). Corynebacterium glutamicum 99,808 17-Jun-97 GB_PAT:I09078 3146 109078 Sequence 4 from Patent WO 8809819. Unknown. 99,617 02-DEC-1994 GB_BA1:BLTHRESYN 1892 Z29563 Brevibacterium lactofermentum; ATCC 13869;; DNA (genomic);. Corynebacterium glutamicum 99,170 20-Sep-95 rxa00335 1554 GB_BA1:CGGLNA 3686 Y13221 Corynebacterium glutamicum glnA gene. Corynebacterium glutamicum 100,000 28-Aug-97 GB_BA2:AF005635 1690 AF005635 Corynebacterium glutamicum glutamine synthetase (glnA) gene, complete cds. Corynebacterium glutamicum 98,906 14-Jun-99 GB_BA1:MSGB27CS 38793 L78817 Mycobacterium leprae cosmid B27 DNA sequence. Mycobacterium leprae 66,345 15-Jun-96 rxa00347 891 GB_EST27:AI455217 624 AI455217 LD21828.3prime LD Drosophila melanogaster embryo pOT2 Drosophila Drosophila melanogaster 34,510 09-MAR-1999 melanogaster cDNA clone LD21828 3prime, mRNA sequence. GB_BA2:SSU30252 2891 U30252 Synechococcus PCC7942 nucleoside diphosphate kinase and ORF2 protein Synechococcus PCC7942 37,084 29-OCT-1999 genes, complete cds, ORF1 protein gene, partial cds, and neutral site I for vector use. GB_EST21:AA911262 581 AA911262 oe75a02 s1 NCI_CGAP_Lu5 Homo sapiens cDNA clone IMAGE:1417418 3′ Homo sapiens 37,500 21-Apr-98 similar to gb:A18757 UROKINASE PLASMINOGEN ACTIVATOR SURFACE RECEPTOR, GPI-ANCHORED (HUMAN);, mRNA sequence. rxa00351 1578 GB_BA1:MLU15187 36138 U15187 Mycobacterium leprae cosmid L296. Mycobacterium leprae 52,972 09-MAR-1995 GB_IN2:AC004373 72722 AC004373 Drosophila melanogaster DNA sequence (P1 DS05273 (D80)), complete Drosophila melanogaster 46,341 17-Jul-98 sequence. GB_IN2:AF145653 3197 AF145653 Drosophila melanogaster clone GH08860 BcDNA.GH08860 Drosophila melanogaster 49,471 14-Jun-99 (BcDNA.GH08860) mRNA, complete cds. rxa00365 727 GB_BA1:AB024708 8734 AB024708 Corynebacterium glutamicum gltB and gltD genes for glutamine 2-oxoglutarate Corynebacterium glutamicum 96,556 13-MAR-1999 aminotransferase large and small subunits, complete cds GB_BA1:MTCY1A6 37751 Z83864 Mycobacterium tuberculosis H37Rv complete genome; segment 159/162. Mycobacterium tuberculosis 39,496 17-Jun-98 GB_BA1:SC3A3 15901 AL109849 Streptomyces coelicolor cosmid 3A3. Streptomyces coelicolor 37,946 16-Aug-99 A3 (2) rxa00366 480 GB_BA1:AB024708 8734 AB024708 Corynebacterium glutamicum gltB and gltD genes for glutamine 2-oxoglutarate Corynebacterium glutamicum 99,374 13-MAR-1999 aminotransferase large and small subunits, complete cds. GB_BA1:MTCY1A6 37751 Z83864 Mycobacterium tuberculosis H37Rv complete genome; segment 159/162. Mycobacterium tuberculosis 41,333 17-Jun-98 GB_BA1:SC3A3 15901 AL109849 Streptomyces coelicolor cosmid 3A3. Streptomyces coelicolor 37,554 16-Aug-99 A3 (2) rxa00367 4653 GB_BA1:AB024708 8734 AB024708 Corynebacterium glutamicum gltB and gltD genes for glutamine 2- Corynebacterium glutamicum 99,312 13-MAR-1999 oxoglutarate aminotransferase large and small subunits, complete cds. GB_BA1:MTCY1A6 37751 Z83864 Mycobacterium tuberculosis H37Rv complete genome; segment 159/162. Mycobacterium tuberculosis 36,971 17-Jun-98 GB_BA1:SC3A3 15901 AL109849 Streptomyces coelicolor cosmid 3A3. Streptomyces coelicolor 37,905 16-Aug-99 A3 (2) rxa00371 1917 GB_VI:SBVORFS 7568 M89923 Sugarcane bacilliform virus ORF 1, 2, and 3 DNA, complete cds. Sugarcane bacilliform virus 35,843 12-Jun-93 GB_EST37:AI967505 380 AI967505 Ljirnpest03-215-c10 Ljirnp Lambda HybriZap two-hybrid library Lotus japonicus Lotus japonicus 42,593 24-Aug-99 cDNA clone LP215-03-c10 5′ similar to 60S ribosomal protein L39, mRNA sequence. GB_IN1:CELK09H9 37881 AF043700 Caenorhabditis elegans cosmid K09H9. Caenorhabditis elegans 34,295 22-Jan-98 rxa00377 1245 GB_BA1:CCU13664 1678 U13664 Caulobacter crescentus uroporphyrinogen decarboxylase homolog (hemE) Caulobacter crescentus 36,832 24-MAR-1995 gene, partial cds. GB_PL1:ANSDGENE 1299 Y08866 A. nidulans sD gene. Emericella nidulans 39,603 17-OCT-1996 GB_GSS4:AQ730303 483 AQ730303 HS_5505_B1 _C04_T7A RPCI-11 Human Male BAC Library Homo sapiens Homo sapiens 36,728 15-Jul-99 genomic clone Plate = 1081 Col = 7 Row = F, genomic survey sequence. rxa00382 1425 GB_BA1:PAHEML 4444 X82072 P. aeruginosa hemL gene. Pseudomonas aeruginosa 54,175 18-DEC-1995 GB_BA1:MTY25D10 40838 Z95558 Mycobacterium tuberculosis H37Rv complete genome; segment 28/162. Mycobacterium tuberculosis 61,143 17-Jun-98 GB_BA1:MSGY224 40051 AD000004 Mycobacterium tuberculosis sequence from clone y224. Mycobacterium tuberculosis 61,143 03-DEC-1996 rxa00383 1467 GB_BA1:MLCB1222 34714 AL049491 Mycobacterium leprae cosmid B1222. Mycobacterium leprae 43,981 27-Aug-99 GB_HTG2:AC006269 167171 AC006269 Homo sapiens chromosome 17 clone hRPK.515_E_23 map 17, *** Homo sapiens 35,444 10-Jun-99 SEQUENCING IN PROGRESS ***, 2 ordered pieces. GB_HTG2:AC007638 178053 AC007638 Homo sapiens chromosome 17 clone hRPK.515_O_17 map 17, *** Homo sapiens 34,821 22-MAY-1999 SEQUENCING IN PROGRESS ***, 8 unordered pieces. rxa00391 843 GB_EST38:AW017053 613 AW017053 EST272398 Schistosoma mansoni male, Phil LoVerde/Joe Merrick Schistosoma mansoni 40,472 10-Sep-99 Schistosoma mansoni cDNA clone SMMAS14 5′ end, mRNA sequence. GB_PAT:AR065852 32207 AR065852 Sequence 20 from U.S. Pat. 5849564. Unknown. 38,586 29-Sep-99 GB_VI:AF148805 28559 AF148805 Kaposi's sarcoma-associated herpesvirus ORF 68 gene, partial cds; and ORF Kaposi's sarcoma-associated 38,509 2-Aug-99 69, kaposin, v-FLIP, v-cyclin, latent nuclear antigen, ORF K14, v-GPCR, herpesvirus putative phosphoribosylformylglycinamidine synthase, and LAMP (LAMP) genes, complete cds. rxa00393 1017 GB_BA1:MTY25D10 40838 Z95558 Mycobacterium tuberculosis H37Rv complete genome; segment 28/162. Mycobacterium tuberculosis 36,308 17-Jun-98 GB_BA1:MSGY224 40051 AD000004 Mycobacterium tuberculosis sequence from clone y224. Mycobacterium tuberculosis 39,282 03-DEC-1996 GB_BA1:MLB1306 7762 Y13803 Mycobacterium leprae cosmid B1306 DNA. Mycobacterium leprae 39,228 24-Jun-97 rxa00402 623 GB_BA2:AF052652 2096 AF052652 Corynebacterium glutamicum homoserine O-acetyltransferase (metA) gene, Corynebacterium glutamicum 99,672 19-MAR-1998 complete cds. GB_BA2:AF109162 4514 AF109162 Corynebacterium diphtheriae heme uptake locus, complete sequence. Corynebacterium diphtheriae 40,830 8-Jun-99 GB_BA2:AF092918 20758 AF092918 Pseudomonas alcaligenes outer membrane Xcp-secretion system gene Pseudomonas alcaligenes 50,161 06-DEC-1998 cluster. rxa00403 1254 GB_BA2:AF052652 2096 AF052652 Corynebacterium glutamicum homoserine O-acetyltransferase (metA) gene, Corynebacterium glutamicum 99,920 19-MAR-1998 complete cds. GB_BA1:MTV016 53662 AL021841 Mycobacterium tuberculosis H37Rv complete genome; segment 143/162. Mycobacterium tuberculosis 52,898 23-Jun-99 GB_EST23:AI111288 750 AI111288 SWOvAMCAQ02A05SK Onchocerca volvulus adult male cDNA (SAW98MLW- Onchocerca volvulus 37,565 31-Aug-98 OvAM) Onchocerca volvulus cDNA clone SWOvAMCAQ02A05 5′, mRNA sequence. rxa00405 613 GB_BA1:MTV016 53662 AL021841 Mycobacterium tuberculosis H37Rv complete genome; segment 143/162. Mycobacterium tuberculosis 57,259 23-Jun-99 GB_PR4:AC005145 143678 AC005145 Homo sapiens Xp22-166-169 GSHB-523A23 (Genome Systems Human BAC Homo sapiens 34,179 08-DEC-1998 library) complete sequence. GB_BA1:MTV016 53662 AL021841 Mycobacterium tuberculosis H37Rv complete genome; segment 143/162. Mycobacterium tuberculosis 40,169 23-Jun-99 rxa00420 1587 GB_BA1:MTY13D12 37085 Z80343 Mycobacterium tuberculosis H37Rv complete genome; segment 156/162. Mycobacterium tuberculosis 62,031 17-Jun-98 GB_BA1:MSGY126 37164 AD000012 Mycobacterium tuberculosis sequence from clone y126. Mycobacterium tuberculosis 61,902 10-DEC-1996 GB_BA1:MSGB971CS 37566 L78821 Mycobacterium leprae cosmid B971 DNA sequence. Mycobacterium leprae 39,651 15-Jun-96 rxa00435 1296 GB_BA1:AFACBBTZ 2760 M68904 Alcaligenes eutrophus chromsomal transketolase (cbb Tc) and Ralstonia eutropha 38,677 27-Jul-94 phosphoglycolate phosphatase (cbbZc) genes, complete cds. GB_HTG4:AC009541 169583 AC009541 Homo sapiens chromosome 7, *** SEQUENCING IN PROGRESS ***, 25 Homo sapiens 36,335 12-OCT-1999 unordered pieces. GB_HTG4:AC009541 169583 AC009541 Homo sapiens chromosome 7, *** SEQUENCING IN PROGRESS ***, 25 Homo sapiens 36,335 12-OCT-1999 unordered pieces. rxa00437 579 GB_PR4:AC005951 155450 AC005951 Homo sapiens chromosome 17, clone hRPK.372_K_20, complete sequence. Homo sapiens 31,738 18-Nov-98 GB_BA1:SC2A11 22789 AL031184 Streptomyces coelicolor cosmid 2A11. Streptomyces coelicolor 43.262 5-Aug-98 GB_PR4:AC005951 155450 AC005951 Homo sapiens chromosome 17, clone hRPK.372_K_20, complete sequence. Homo sapiens 37,647 18-Nov-98 rxa00439 591 GB_BA1:MTV016 53662 AL021841 Mycobacterium tuberculosis H37Rv complete genome; segment 143/162. Mycobacterium tuberculosis 37,088 23-Jun-99 GB_PL2:AF167358 1022 AF167358 Rumex acetosa expansin (EXP3) gene, partial cds. Rumex acetosa 46,538 17-Aug-99 GB_HTG3:AC009120 269445 AC009120 Homo sapiens chromosome 16 clone RPCI-11_484E3, *** SEQUENCING IN Homo sapiens 43,276 3-Aug-99 PROGRESS ***, 34 unordered pieces. rxa00440 582 GB_BA2:SKZ86111 7860 Z86111 Streptomyces lividans rpsP, trmD, rpIS, sipW, sipX, sipY, sipZ, mutT genes Streptomyces lividans 43,080 27-OCT-1999 and 4 open reading frames. GB_BA1:SC2E1 38962 AL023797 Streptomyces coelicolor cosmid 2E1. Streptomyces coelicolor 42,931 4-Jun-98 GB_BA1:SC2E1 38962 AL023797 Streptomyces coelicolor cosmid 2E1. Streptomyces coelicolor 36,702 4-Jun-98 rxa00441 1287 GB_PR2:HS173D1 117338 AL031984 Human DNA sequence from clone 173D1 on chromosome 1p36.21- Homo sapiens 38,027 23-Nov-99 36.33.Contains ESTs, STSs and GSSs, complete sequence. GB_HTG2:HSDJ719K3 267114 AL109931 Homo sapiens chromosome X clone RP4-719K3 map q21.1-21.31, *** Homo sapiens 34,521 03-DEC-1999 SEQUENCING IN PROGRESS ***, in unordered pieces. GB_HTG2:HSDJ719K3 267114 AL109931 Homo sapiens chromosome X clone RP4-719K3 map q21.1-21.31, *** Homo sapiens 34,521 03-DEC-1999 SEQUENCING IN PROGRESS ***, in unordered pieces. rxa00446 987 GB_BA1:SCD78 36224 AL034355 Streptomyces coelicolor cosmid D78. Streptomyces coelicolor 56,410 26-Nov-98 GB_HTG4:AC009367 226055 AC009367 Drosophila melanogaster chromosome 3L/76A2 clone RPCI98-48B15, *** Drosophila melanogaster 34,959 16-OCT-1999 SEQUENCING IN PROGRESS ***, 44 unordered pieces. GB_HTG4:AC009367 226055 AC009367 Drosophila melanogaster chromosome 3L/76A2 clone RPCI98-48B15, *** Drosophila melanogaster 34,959 16-OCT-1999 SEQUENCING IN PROGRESS ***, 44 unordered pieces. rxa00448 1143 GB_PR3:AC003670 88945 AC003670 Homo sapiens 12q13.1 PAC RPCI1-130F5 (Roswell Park Cancer Institute Homo sapiens 35,682 9-Jun-98 Human PAC library) complete sequence. GB_HTG2:AF029367 148676 AF029367 Homo sapiens chromosome 12 clone RPCI-1 130F5 map 12q13.1, *** Homo sapiens 31,373 18-OCT-1997 SEQUENCING IN PROGRESS ***, 156 unordered pieces. GB_HTG2:AF029367 148676 AF029367 Homo sapiens chromosome 12 clone RPCI-1 130F5 map 12q13.1, *** Homo sapiens 31,373 18-OCT-1997 SEQUENCING IN PROGRESS ***, 156 unordered pieces. rxa00450 424 GB_HTG2:AC007824 133361 AC007824 Drosophila melanogaster chromosome 3 clone BACR02L16 (D715) RPCI-98 Drosophila melanogaster 40,000 2-Aug-99 02.L.16 map 89E-90A strain y; cn bw sp, *** SEQUENCING IN PROGRESS ***, 91 unordered pieces. GB_HTG2:AC007824 133361 AC007824 Drosophila melanogaster chromosome 3 clone BACR02L16 (D715) RPCI-98 Drosophila melanogaster 40,000 2-Aug-99 02.L.16 map 89E-90A strain y, cn bw sp, *** SEQUENCING IN PROGRESS ***, 91 unordered pieces. GB_EST35:AI818057 412 AI818057 wk14a08.x1 NCI_CGAP_Lym12 Homo sapiens cDNA clone IMAGE:2412278 Homo sapiens 35,714 24-Aug-99 3′ similar to gb:Y00764 UBIQUINOL-CYTOCHROME C REDUCTASE 11 KD PROTEIN (HUMAN);, mRNA sequence. rxa00461 975 GB_BA1:MLCB1779 43254 Z98271 Mycobacterium leprae cosmid B1779. Mycobacterium leprae 39,308 8-Aug-97 GB_IN1:DMC86E4 29352 AL021086 Drosophila melanogaster cosmid clone 86E4. Drosophila melanogaster 37,487 27-Apr-99 GB_GSS15:AQ640325 467 AQ640325 927P1-2H3.TP 927P1 Trypanosoma brucei genomic clone 927P1-2H3, Trypanosoma brucei 38,116 8-Jul-99 genomic survey sequence. rxa00465 rxa00487 1692 GB_BA1:BAGUAA 3866 Y10499 B. ammoniagenes guaA gene. Corynebacterium 74,259 8-Jan-98 ammoniagenes GB_BA2:U00015 42325 U00015 Mycobacterium leprae cosmid B1620. Mycobacterium leprae 37,248 01-Mar-1994 GB_BA1:MTCY78 33818 Z77165 Mycobacterium tuberculosis H37Rv complete genome, segment 145/162. Mycobacterium tuberculosis 39,725 17-Jun-98 rxa00488 1641 GB_BA1:MTCY78 33818 Z77165 Mycobacterium tuberculosis H37Rv complete genome; segment 145/162. Mycobacterium tuberculosis 39,451 17-Jun-98 GB_BA2:U00015 42325 U00015 Mycobacterium leprae cosmid B1620. Mycobacterium leprae 39,178 01-Mar-1994 GB_BA1:SCAJ10601 4692 AJ010601 Streptomyces coelicolor A3 (2) DNA for whiD and whiK loci. Streptomyces coelicolor 60,835 17-Sep-98 rxa00489 1245 GB_BA2:U00015 42325 U00015 Mycobacterium leprae cosmid B1620. Mycobacterium leprae 38,041 01-Mar-1994 GB_HTG2:HS225E12 126464 AL031772 Homo sapiens chromosome 6 clone RP1-225E12 map q24, *** SEQUENCING Homo sapiens 36,756 03-DEC-1999 IN PROGRESS ***, in unordered pieces. GB_HTG2:HS225E12 126464 AL031772 Homo sapiens chromosome 6 clone RP1-225E12 map q24, *** SEQUENCING Homo sapiens 36,756 03-DEC-1999 IN PROGRESS ***, in unordered pieces. rxa00533 1155 GB_BA1:CGLYS 2803 X57226 C. glutamicum lysC-alpha, lysC-beta and asd genes for aspartokinase-alpha Corynebacterium glutamicum 99,913 17-Feb-97 and -beta subunits, and aspartate beta semialdehyde dehydrogenase, respectively (EC 2.7.2.4; EC 1.2.1.11) GB_BA1:CGCYSCASD 1591 X82928 C. glutamicum aspartate-semialdehyde dehydrogenase gene. Corynebacterium glutamicum 99,221 17-Feb-97 GB_PAT:A07546 2112 A07546 Recombinant DNA fragment (Pstl-Xhol). synthetic construct 99,391 30-Jul-93 rxa00534 1386 GB_BA1:CGLYS 2803 X57226 C. glutamicum lysC-alpha, lysC-beta and asd genes for aspartokinase-alpha Corynebacterium glutamicum 99,856 17-Feb-97 and -beta subunits, and aspartate beta semialdehyde dehydrogenase, respectively (EC 2.7.2.4; EC 1.2.1.11). GB_BA1:CORASKD 2957 L16848 Corynebacterium flavum aspartokinase (ask), and aspartate-semialdehyde Corynebacterium flavescens 98,701 11-Jun-93 dehydrogenase (asd) genes, complete cds. GB_PAT:E14514 1643 E14514 DNA encoding Brevibacterium aspartokinase. Corynebacterium glutamicum 98,773 28-Jul-99 rxa00536 1494 GB_BA1:CGLEUA 3492 X70959 C. glutamicum gene leuA for isopropylmalate synthase. Corynebacterium glutamicum 100,000 10-Feb-99 GB_BA1:MTV025 121125 AL022121 Mycobacterium tuberculosis H37Rv complete genome; segment 155/162. Mycobacterium tuberculosis 68,003 24-Jun-99 GB_BA1:MTU88526 2412 U88526 Mycobacterium tuberculosis putative alpha-isopropyl malate synthase (leuA) Mycobacterium tuberculosis 68,185 26-Feb-97 gene, complete cds. rxa00537 2409 GB_BA2:SCD25 41622 AL118514 Streptomyces coelicolor cosmid D25. Streptomyces coelicolor 63,187 21-Sep-99 A3 (2) GB_BA1:MTCY7H7A 10451 Z95618 Mycobacterium tuberculosis H37Rv complete genome; segment 39/162. Mycobacterium tuberculosis 62,401 17-Jun-98 GB_BA1:MTU34956 2462 U34956 Mycobacterium tuberculosis phosphoribosylformylglycinamidine synthase Mycobacterium tuberculosis 62,205 28-Jan-97 (purL) gene, complete cds. rxa00541 792 GB_PAT:I92052 2115 I92052 Sequence 19 from U.S. Pat. 5726299. Unknown. 98,359 01-DEC-1998 GB_BA1:MLCB5 38109 Z95151 Mycobacterium leprae cosmid B5. Mycobacterium leprae 62,468 24-Jun-97 GB_BA1:MTCY369 36850 Z80226 Mycobacterium tuberculosis H37Rv complete genome; segment 36/162. Mycobacterium tuberculosis 60,814 17-Jun-98 rxa00558 1470 GB_BA1:BAPURF 1885 X91252 B. ammoniagenes purF gene Corynebacterium 66,095 5-Jun-97 ammoniagenes GB_BA1:MLU15182 40123 U15182 Mycobacterium leprae cosmid B2266. Mycobacterium leprae 64,315 09-MAR-1995 GB_BA1:MTCY7H7A 10451 Z95618 Mycobacterium tuberculosis H37Rv complete genome; segment 39/162. Mycobacterium tuberculosis 64,863 17-Jun-98 rxa00579 1983 GB_PAT:AR016483 2104 AR016483 Sequence 1 from U.S. Pat. 5776740 Unknown. 98,810 05-DEC-1998 EM_PAT:E11273 2104 E11273 DNA encoding serine hydroxymethyl transferase. Corynebacterium glutamicum 98,810 08-OCT-1997 (Rel. 52, Created) GB_PAT:E12594 2104 E12594 DNA encoding serine hydroxymethyltransferase from Brevibacterium flavum. Corynebacterium glutamicum 98,810 24-Jun-98 rxa00580 1425 GB_PAT:E12594 2104 E12594 DNA encoding serine hydroxymethyltransferase from Brevibacterium flavum. Corynebacterium glutamicum 99,368 24-Jun-98 GB_PAT:AR016483 2104 AR016483 Sequence 1 from U.S. Pat. 5776740. Unknown. 99,368 05-DEC-1998 EM_PAT:E11273 2104 E11273 DNA encoding serine hydroxymethyl transferase. Corynebacterium glutamicum 99,368 08-OCT-1997 (Rel. 52, Created) rxa00581 1092 GB_PAT:E12594 2104 E12594 DNA encoding serine hydroxymethyltransferase from Brevibacterium flavum. Corynebacterium glutamicum 37,071 24-Jun-98 EM_PAT:E11273 2104 E11273 DNA encoding serine hydroxymethyl transferase. Corynebacterium glutamicum 37,071 08-OCT-1997 (Rel. 52, Created) GB_PAT:AR016483 2104 AR016483 Sequence 1 from U.S. Pat. 5776740. Unknown. 37,071 05-DEC-1998 rxa00584 1248 GB_BA1:CORAHPS 2570 L07603 Corynebacterium glutamicum 3-deoxy-D-arabinoheptulosonate-7-phosphate Corynebacterium glutamicum 98,236 26-Apr-93 synthase gene, complete cds. GB_BA1:AOPCZA361 37941 AJ223998 Amycolatopsis orientalis cosmid PCZA361. Amycolatopsis orientalis 54,553 29-MAR-1999 GB_BA1:D90714 14358 D90714 Escherichia coil genomic DNA. (16.8-17.1 min). Escherichia coli 53,312 7-Feb-99 rxa00618 1230 GB_EST19:AA802737 280 AA802737 GM06236.5prime GM Drosophila melanogaster ovary BlueScript Drosophila Drosophila melanogaster 39,928 25-Nov-98 melanogaster cDNA clone GM06236 5prime, mRNA sequence. GB_EST28:AI534381 581 AI534381 SD07186.5prime SD Drosophila melanogaster Schneider L2 cell culture pOT2 Drosophila melanogaster 41,136 18-MAR-1999 Drosophila melanogaster cDNA clone SD07186 5prime similar to X89858: Ani FBgn0011558 PID:g927407 SPTREMBL:Q24240, mRNA sequence. GB_IN1:DMANILLIN 4029 X89858 D. melanogaster mRNA for anillin protein. Drosophila melanogaster 34,398 8-Nov-95 rxa00619 1551 GB_BA1:MTCY369 36850 Z80226 Mycobacterium tuberculosis H37Rv complete genome; segment 36/162. Mycobacterium tuberculosis 62,776 17-Jun-98 GB_BA1:MLCB5 38109 Z95151 Mycobacterium leprae cosmid B5. Mycobacterium leprae 61,831 24-Jun-97 GB_PAT:A60305 1845 A60305 Sequence 5 from Patent WO9708323. unidentified 61,785 06-MAR-1998 rxa00620 1014 GB_PL2:AF063247 1450 AF063247 Pneumocystis carinii f. sp. ratti enolase mRNA, complete cds. Pneumocystis carinii f. sp. 41,060 5-Jan-99 ratti GB_BA1:STMAPP 2069 M91546 Streptomyces lividans aminopeptidase P (PepP) gene, complete cds. Streptomyces lividans 37,126 12-Jun-93 GB_HTG3:AC008763 214575 AC008763 Homo sapiens chromosome 19 clone CITB-E1_3214H19, *** SEQUENCING Homo sapiens 40,020 3-Aug-99 IN PROGRESS ***, 21 unordered pieces. rxa00624 810 GB_IN1:CEY41E3 150641 Z95559 Caenorhabditis elegans cosmid Y41E3, complete sequence. Caenorhabditis elegans 36,986 2-Sep-99 GB_EST13:AA362167 372 AA362167 EST71561 Macrophage I Homo sapiens cDNA 5′ end, mRNA sequence. Homo sapiens 38,378 21-Apr-97 GB_IN1:CEY41E3 150641 Z95559 Caenorhabditis elegans cosmid Y41E3, complete sequence. Caenorhabditis elegans 37,694 2-Sep-99 rxa00626 1386 GB_BA1:MTCY369 36850 Z80226 Mycobacterium tuberculosis H37Rv complete genome; segment 36/162. Mycobacterium tuberculosis 57,971 17-Jun-98 GB_BA1:MLCB5 38109 Z95151 Mycobacterium leprae cosmid B5. Mycobacterium leprae 58,806 24-Jun-97 GB_BA1:MLU15187 36138 U15187 Mycobacterium leprae cosmid L296. Mycobacterium leprae 38,007 09-MAR-1995 rxa00632 795 GB_BA1:BRLBIOAD 2272 D14083 Brevibacterium flavum genes for 7,8-diaminopelargonic acid aminotransferase Corynebacterium glutamicum 97,358 3-Feb-99 and dethiobiotin synthetase, complete cds. GB_PAT:E04041 675 E04041 DNA sequence coding for desthiobiotinsynthetase. Corynebacterium glutamicum 98,074 29-Sep-97 GB_PAT:E04040 1272 E04040 DNA sequence coding for diamino pelargonic acid aminotransferase. Corynebacterium glutamicum 93,814 29-Sep-97 rxa00633 1392 GB_BA1:BRLBIOAD 2272 D14083 Brevibacterium flavum genes for 7,8-diaminopelargonic acid aminotransferase Corynebacterium glutamicum 95,690 3-Feb-99 and dethiobiotin synthetase, complete cds. GB_PAT:E04040 1272 E04040 DNA sequence coding for diamino pelargonic acid aminotransferase. Corynebacterium glutamicum 95,755 29-Sep-97 GB_BA2:EHU38519 1290 U38519 Erwinia herbicola adenosylmethionine-8-amino-7-oxononanoate transaminase Erwinia herbicola 55,564 4-Nov-96 (bioA) gene, complete cds. rxa00688 666 GB_BA1:MTV041 28826 AL021958 Mycobacterium tuberculosis H37Rv complete genome; segment 35/162. Mycobacterium tuberculosis 60,030 17-Jun-98 GB_BA1:BRLSECY 1516 D14162 Brevibacterium flavum gene for SecY protein (complete cds) and gene or Corynebacterium glutamicum 99,563 3-Feb-99 adenylate kinase (partial cds). GB_BA2:MBU77912 7163 U77912 Mycobacterium bovis MBE50a gene, partial cds; and MBE50b, MBE50c, Mycobacterium bovis 60,030 27-Jan-99 preprotein translocase SecY subunit (secY), adenylate kinase (adk), methionine aminopeptidase (map), RNA polymerase ECF sigma factor (sigE50), MBE50d, and MBE50e genes, complete cds. rxa00708 930 GB_BA2:AF157493 25454 AF157493 Zymomonas mobilis ZM4 fosmid clone 42D7, complete sequence. Zymomonas mobilis 39,116 5-Jul-99 GB_PAT:I00836 1853 I00836 Sequence 1 from Patent US 4758514. Unknown 47,419 21-May-1993 GB_PAT:E00311 1853 E00311 DNA coding of 2,5-diketogluconic acid reductase. unidentified 47,419 29-Sep-97 rxa00717 1083 GB_PAT:I78753 1187 I78753 Sequence 9 from U.S. Pat. 5693781. Unknown. 37,814 3-Apr-98 GB_PAT:I92042 1187 I92042 Sequence 9 from U.S. Pat. 5726299. Unknown 37,814 01-DEC-1998 GB_BA1:MTCI125 37432 Z98268 Mycobacterium tuberculosis H37Rv complete genome; segment 76/162. Mycobacterium tuberculosis 50,647 17-Jun-98 rxa00718 831 GB_BA1:MTCI125 37432 Z98268 Mycobacterium tuberculosis H37Rv complete genome; segment 76/162. Mycobacterium tuberculosis 55,228 17-Jun-98 GB_BA1:MTCI125 37432 Z98268 Mycobacterium tuberculosis H37Rv complete genome; segment 76/162 Mycobacterium tuberculosis 40,300 17-Jun-98 GB_GSS12:AQ420755 671 AQ420755 RPCI-11-168G18.TJ RPCI-11 Homo sapiens genomic clone RPCI-11- Homo sapiens 35,750 23-MAR-1999 168G18, genomic survey sequence. rxa00727 1035 GB_HTG3:AC008332 118545 AC008332 Drosophila melanogaster chromosome 2 clone BACR48D10 (D867) RPCI-98 Drosophila melanogaster 40,634 6-Aug-99 48.D.10 map 34A-34A strain y; cn bw sp, *** SEQUENCING IN PROGRESS ***, 78 unordered pieces. GB_HTG3:AC008332 118545 AC008332 Drosophila melanogaster chromosome 2 clone BACR48D10 (D867) RPCI-98 Drosophila melanogaster 40,634 6-Aug-99 48.D.10 map 34A-34A strain y; cn bw sp, *** SEQUENCING IN PROGRESS***, 78 unordered pieces. GB_HTG3:AC008332 118545 AC008332 Drosophila melanogaster chromosome 2 clone BACR48D10 (D867) RPCI-98 Drosophila melanogaster 33,888 6-Aug-99 48.D.10 map 34A-34A strain y; cn bw sp, *** SEQUENCING IN PROGRESS***, 78 unordered pieces. rxa00766 966 GB_HTG2:AC006789 83823 AC006789 Caenorhabditis elegans clone Y49F6, *** SEQUENCING IN PROGRESS ***, 2 Caenorhabditis elegans 36,737 25-Feb-99 unordered pieces. GB_HTG2:AC006789 83823 AC006789 Caenorhabditis elegans clone Y49F6, *** SEQUENCING IN PROGRESS ***, 2 Caenorhabditis elegans 36,737 25-Feb-99 unordered pieces. GB_BA1:D90810 20476 D90810 E. coli genomic DNA, Kohara clone #319 (37.4-37.8 min.). Escherichia coli 36,526 29-MAY-1997 rxa00770 1293 GB_BA1:MTV043 68848 AL022004 Mycobacterium tuberculosis H37Rv complete genome; segment 40/162. Mycobacterium tuberculosis 66,193 24-Jun-99 GB_BA1:MLU15182 40123 U15182 Mycobacterium leprae cosmid B2266. Mycobacterium leprae 61,443 09-MAR-1995 GB_BA2:SCD25 41622 AL118514 Streptomyces coelicolor cosmid D25. Streptomyces coelicolor 59,938 21-Sep-99 A3 (2) rxa00779 1056 GB_HTG1:CER08A5 51920 Z82281 Caenorhabditis elegans chromosome V clone R08A5, *** SEQUENCING IN Caenorhabditis elegans 64,896 14-OCT-1998 PROGRESS ***, in unordered pieces. GB_HTG1:CER08A5 51920 Z82281 Caenorhabditis elegans chromosome V clone R08A5, *** SEQUENCING IN Caenorhabditis elegans 64,896 14-OCT-1998 PROGRESS ***, in unordered pieces. GB_PL2:AF078693 1492 AF078693 Chlamydomonas reinhardtii putative O-acetylserine (thiol)lyase precursor Chlamydomonas reinhardtii 57,970 3-Nov-99 (Crcys-1A) mRNA, nuclear gene encoding organellar protein, complete cds. rxa00780 669 GB_BA1:MTCY98 31225 Z83860 Mycobacterium tuberculosis H37Rv complete genome; segment 103/162. Mycobacterium tuberculosis 54,410 17-Jun-98 GB_BA1:AVINIFREG 7099 M60090 Azotobacter chroococcum nifU, nifS, nifV, nifP, nifW, nifZ and nifM genes, Azotobacter chroococcum 51,729 26-Apr-93 complete cds. GB_BA2:AF001780 6701 AF001780 Cyanothece PCC 8801 NifP (nifP), nitrogenase (nifB), FdxN (fdxN), NifS (nifS) Cyanothece PCC8801 36,309 08-MAR-1999 and NifU (nifU) genes, complete cds, and NifH (nifH) gene, partial cds. rxa00838 1023 GB_EST1:Z30506 329 Z30506 ATTS2430 AC16H Arabidopsis thaliana cDNA clone TAI306 3′, mRNA Arabidopsis thaliana 44,308 11-MAR-1994 sequence. GB_PL2:AC006258 110469 AC006258 Arabidopsis thaliana BAC F18G18 from chromosome V near 60.5 cM, Arabidopsis thaliana 35,571 28-DEC-1998 complete sequence. GB_EST37:AI998439 455 AI998439 701545695 A. thaliana, Columbia Col-0, rosette-2 Arabidopsis thaliana cDNA Arabidopsis thaliana 36,044 8-Sep-99 clone 701545695, mRNA sequence. rxa00863 867 GB_BA1:BLDAPAB 3572 Z21502 B. lactofermentum dapA and dapB genes for dihydrodipicolinate synthase and Corynebacterium glutamicum 99,539 16-Aug-93 dihydrodipicolinate reductase. GB_PAT:E16749 2001 E16749 gDNA encoding dihydrodipicolinate synthase (DDPS). Corynebacterium glutamicum 99,539 28-Jul-99 GB_PAT:E14520 2001 E14520 DNA encoding Brevibacterium dihydrodipicolinic acid synthase. Corynebacterium glutamicum 99,539 28-Jul-99 rxa00864 873 GB_BA1:BLDAPAB 3572 Z21502 B. lactofermentum dapA and dapB genes for dihydrodipicolinate synthase and Corynebacterium glutamicum 99,885 16-Aug-93 dihydrodipicolinate reductase. GB_BA1:CGDAPB 1902 X67737 C. glutamicum dapB gene for dihydrodipicolinate reductase. Corynebacterium glutamicum 100,000 1-Apr-93 GB_PAT:E14520 2001 E14520 DNA encoding Brevibacterium dihydrodipicolinic acid synthase. Corynebacterium glutamicum 100,000 28-Jul-99 rxa00865 1026 GB_BA1:BLDAPAB 3572 Z21502 B. lactofermentum dapA and dapB genes for dihydrodipicolinate synthase and Corynebacterium glutamicum 100,000 16-Aug-93 dihydrodipicolinate reductase. GB_PAT:E16752 1411 E16752 gDNA encoding dihydrodipicolinate reductase (DDPR). Corynebacterium glutamicum 99,805 28-Jul-99 GB_PAT:AR038113 1411 AR038113 Sequence 18 from U.S. Pat. 5804414. Unknown. 99,805 29-Sep-99 rxa00867 650 GB_BA1:MTV002 56414 AL008967 Mycobacterium tuberculosis H37Rv complete genome; segment 122/162. Mycobacterium tuberculosis 39,179 17-Jun-98 GB_BA1:MLCB22 40281 Z98741 Mycobacterium leprae cosmid B22. Mycobacterium leprae 39,482 22-Aug-97 GB_BA1:SAU19858 2838 U19858 Streptomyces antibioticus guanosine pentaphosphate synthetase (gpsl) gene, Streptomyces antibioticus 69,706 25-OCT-1996 complete cds. rxa00873 779 GB_BA1:SCO001206 9184 AJ001206 Streptomyces coelicolor A3 (2), glycogen metabolism cluster II. Streptomyces coelicolor 63,415 29-MAR-1999 GB_BA1:SCO001205 9589 AJ001205 Streptomyces coelicolor A3 (2) glycogen metabolism cluster I. Streptomyces coelicolor 61,617 29-MAR-1999 GB_BA1:D78198 2304 D78198 Pimelobacter sp. DNA for trehalose synthase, complete cds. Pimelobacter sp. 60,594 5-Feb-99 rxa00884 1263 GB_BA1:MTCY253 41230 Z81368 Mycobacterium tuberculosis H37Rv complete genome; segment 106/162. Mycobacterium tuberculosis 37,785 17-Jun-98 GB_BA1:MSGY222 41156 AD000010 Mycobacterium tuberculosis sequence from clone y222. Mycobacterium tuberculosis 38,006 03-DEC-1996 GB_GSS15:AQ654600 468 AQ654600 Sheared DNA-1O14. TF Sheared DNA Trypanosoma brucei genomic clone Trypanosoma brucei 33,974 22-Jun-99 Sheared DNA-1O14, genomic survey sequence. rxa00891 1102 GB_BA1:MTCI418B 11700 Z96071 Mycobacterium tuberculosis H37Rv complete genome; segment 7/162. Mycobacterium tuberculosis 63,297 18-Jun-98 GB_BA1:SCO001206 9184 AJ001206 Streptomyces coelicolor A3 (2), glycogen metabolism cluster II. Streptomyces coelicolor 61,965 29-MAR-1999 GB_BA1:SCO001205 9589 AJ001205 Streptomyces coelicolor A3 (2) glycogen metabolism cluster I Streptomyces coelicolor 61,727 29-MAR-1999 rxa00952 963 EM_PAT:E10963 3118 E10963 gDNA encoding tryptophan synthase. Corynebacterium glutamicum 99,688 08-OCT-1997 (Rel. 52, Created) GB_BA1:BLTRP 7725 X04960 Brevibacterium lactofermentum tryptophan operon. Corynebacterium glutamicum 98,847 10-Feb-99 GB_PAT:E01688 7725 E01688 Genomic DNA of trp operon of prepibacterium latophelmentamn. unidentified 98,428 29-Sep-97 rxa00954 644 GB_PAT:E01375 7726 E01375 DNA sequence of tryptophan operon. Corynebacterium glutamicum 98,758 29-Sep-97 GB_PAT:E01688 7725 E01688 Genomic DNA of trp operon of prepibacterium latophelmentamn. unidentified 98,758 29-Sep-97 GB_BA1:BLTRP 7725 X04960 Brevibacterium lactofermentum tryptophan operon. Corynebacterium glutamicum 98,758 10-Feb-99 rxa00955 1545 GB_PAT:E01375 7726 E01375 DNA sequence of tryptophan operon. Corynebacterium glutamicum 98,372 29-Sep-97 GB_BA1:BLTRP 7725 X04960 Brevibacterium lactofermentum tryptophan operon. Corynebacterium glutamicum 98,372 10-Feb-99 GB_PAT:E01688 7725 E01688 Genomic DNA of trp operon of prepibacterium latophelmentamn. unidentified 98,242 29-Sep-97 rxa00956 1237 EM_PAT:E10963 3118 E10963 gDNA encoding tryptophan synthase. Corynebacterium glutamicum 98,949 08-OCT-1997 (Rel. 52, Created) GB_BA1:BLTRP 7725 X04960 Brevibacterium lactofermentum tryptophan operon. Corynebacterium glutamicum 99,107 10-Feb-99 GB_PAT:E01375 7726 E01375 DNA sequence of tryptophan operon. Corynebacterium glutamicum 98,945 29-Sep-97 rxa00957 1677 GB_BA1:BLTRP 7725 X04960 Brevibacterium lactofermentum tryptophan operon. Corynebacterium glutamicum 99,165 10-Feb-99 GB_PAT:E01375 7726 E01375 DNA sequence of tryptophan operon. Corynebacterium glutamicum 98,927 29-Sep-97 GB_PAT:E01688 7725 E01688 Genomic DNA of trp operon of prepibacterium latophelmentamn. unidentified 98,867 29-Sep-97 rxa00958 747 GB_BA1:BLTRP 7725 X04960 Brevibacterium lactofermentum tryptophan operon. Corynebacterium glutamicum 98,792 10-Feb-99 GB_PAT:E01375 7726 E01375 DNA sequence of tryptophan operon. Corynebacterium glutamicum 98,792 29-Sep-97 GB_PAT:E01688 7725 E01688 Genomic DNA of trp operon of prepibacterium latophelmentamn. unidentified 98,658 29-Sep-97 rxa00970 1050 GB_BA1:CGHOMTHR 3685 Y00546 Corynebacterium glutamicum hom-thrB genes for homoserine dehydrogenase Corynebacterium glutamicum 99,905 12-Sep-93 and homoserine kinase. GB_PAT:I09077 3685 I09077 Sequence 1 from Patent WO 8809819. Unknown. 99,810 02-DEC-1994 GB_PAT:E01358 2615 E01358 DNA encoding for homoserine dehydrogenase (HDH) and homoserine Corynebacterium glutamicum 97,524 29-Sep-97 kinase (HK). rxa00972 1458 GB_PAT:E16755 3579 E16755 gDNA encoding diaminopimelate decarboxylase (DDC) and arginyl-tRNA Corynebacterium glutamicum 99,931 28-Jul-99 synthase. GB_PAT:AR038110 3579 AR038110 Sequence 15 from U.S. Pat. 5804414. Unknown. 99,931 29-Sep-99 GB_PAT:E14508 3579 E14508 DNA encoding Brevibacterium diaminopimelic acid decarboxylase and arginyl- Corynebacterium glutamicum 99,931 28-Jul-99 tRNA synthase. rxa00981 753 GB_OV:GGA245664 512 AJ245664 Gallus gallus partial mRNA for ATP-citrate lyase (ACL gene). Gallus gallus 37,538 28-Sep-99 GB_PL2:AC007887 159434 AC007887 Genomic sequence for Arabidopsis thaliana BAC F15O4 from chromosome I, Arabidopsis thaliana 37,600 04-OCT-1999 complete sequence. GB_GSS1:CNS00RNW 542 AL087338 Arabidopsis thaliana genome survey sequence T7 end of BAC F14D7 of IGF Arabidopsis thaliana 41,264 28-Jun-99 library from strain Columbia of Arabidopsis thaliana , genomic survey sequence. rxa00989 1644 GB_BA1:MTV008 63033 AL021246 Mycobacterium tuberculosis H37Rv complete genome, segment 108/162. Mycobacterium tuberculosis 40,773 17-Jun-98 GB_BA1:SCVALSFP 3619 Y13070 S. coelicolor valS, fpgs, ndk genes. Streptomyces coelicolor 58,119 03-MAR-1998 GB_BA1:MTV008 63033 AL021246 Mycobacterium tuberculosis H37Rv complete genome; segment 108/162. Mycobacterium tuberculosis 38,167 17-Jun-98 rxa00997 705 GB_BA2:CGU31225 1817 U31225 Corynebacterium glutamicum L-proline:NADP + 5-oxidoreductase (proC) gene, Corynebacterium glutamicum 40,841 2-Aug-96 complete cds. GB_HTG1:CEY39C12 282838 AL009026 Caenorhabditis elegans chromosome IV clone Y39C12, *** SEQUENCING IN Caenorhabditis elegans 36,416 26-OCT-1999 PROGRESS ***, in unordered pieces. GB_IN1:CEB0001 39416 Z69634 Caenorhabditis elegans cosmid B0001, complete sequence. Caenorhabditis elegans 36,416 2-Sep-99 rxa01019 1110 GB_HTG2:AC005052 144734 AC005052 Homo sapiens clone RG038K21, *** SEQUENCING IN PROGRESS ***, 3 Homo sapiens 39,172 12-Jun-98 unordered pieces. GB_HTG2:AC005052 144734 AC005052 Homo sapiens clone RG038K21, *** SEQUENCING IN PROGRESS ***, 3 Homo sapiens 39,172 12-Jun-98 unordered pieces. GB_GSS9:AQ171808 512 AQ171808 HS_3179_A1_G03_T7 CIT Approved Human Genomic Sperm Library D Homo Homo sapiens 34,661 17-OCT-1998 sapiens genomic clone Plate = 3179 Col = 5 Row = M, genomic survey sequence. rxa01026 1782 GB_BA1:SC1C2 42210 AL031124 Streptomyces coelicolor cosmid 1C2. Streptomyces coelicolor 68,275 15-Jan-99 GB_BA1:ATLEUCD 2982 X84647 A. teichomyceticus leuC and leuD genes. Actinoplanes teichomyceticus 65,935 04-OCT-1995 GB_BA1:MTV012 70287 AL021287 Mycobacterium tuberculosis H37Rv complete genome; segment 132/162. Mycobacterium tuberculosis 40,454 23-Jun-99 rxa01027 1131 GB_BA1:MLCB637 44882 Z99263 Mycobacterium leprae cosmid B637. Mycobacterium leprae 38,636 17-Sep-97 GB_BA1:MTCY349 43523 Z83018 Mycobacterium tuberculosis H37Rv 3complete genome, segment 131/162. Mycobacterium tuberculosis 51,989 17-Jun-98 GB_BA1:SPUNGMUTX 1172 Z21702 S. pneumoniae ung gene and mutX genes encoding uracil-DNA glycosylase Streptococcus pneumoniae 38,088 15-Jun-94 and 8-oxodGTP nucleoside triphosphatase. rxa01073 954 GB_BA1:BACOUTB 1004 M15811 Bacillus subtilis outB gene encoding a sporulation protein, complete cds. Bacillus subtilis 53,723 26-Apr-93 GB_PR4:AC007938 167237 AC007938 Homo sapiens clone UWGC djs201 from 7q31, complete sequence. Homo sapiens 34,322 1-Jul-99 GB_PL2:ATAC006282 92577 AC006282 Arabidopsis thaliana chromosome II BAC F13K3 genomic sequence, complete Arabidopsis thaliana 36,181 13-MAR-1999 sequence. rxa01079 2226 GB_BA2:AF112535 4363 AF112535 Corynebacterium glutamicum putative glutaredoxin NrdH (nrdH), Nrdl (nrdl), Corynebacterium glutamicum 99,820 5-Aug-99 and ribonucleotide reductase alpha-chain (nrdE) genes, complete cds. GB_BA1:CANRDFGEN 6054 Y09572 Corynebacterium ammoniagenes nrdH, nrdI, nrdE, nrdF genes. Corynebacterium 75,966 18-Apr-98 ammoniagenes GB_BA1:MTV012 70287 AL021287 Mycobacterium tuberculosis H37Rv complete genome; segment 132/162. Mycobacterium tuberculosis 38,296 23-Jun-99 rxa01080 567 GB_BA2:AF112535 4363 AF112535 Corynebacterium glutamicum putative glutaredoxin NrdH (nrdH), NrdI (nrdI), Corynebacterium glutamicum 100,000 5-Aug-99 and ribonucleotide reductase alpha-chain (nrdE) genes, complete cds. GB_BA1:CANRDFGEN 6054 Y09572 Corynebacterium ammoniagenes nrdH, nrdI, nrdE, nrdF genes. Corynebacterium 65,511 18-Apr-98 ammoniagenes GB_BA1:STNRD 4894 X73226 S. typhimurium nrdEF operon. Salmonella typhimurium 52,477 03-MAR-1997 rxa01087 999 GB_IN2:AF063412 1093 AF063412 Limnadia lenticularis elongation factor 1-alpha mRNA, partial cds. Limnadia lenticularis 43,750 29-MAR-1999 GB_PR3:HS24M15 134539 Z94055 Human DNA sequence from PAC 24M15 on chromosome 1. Contains Homo sapiens 37,475 23-Nov-99 tenascin-R (restrictin), EST. GB_IN2:ARU85702 1240 U85702 Anathix ralla elongation factor-1 alpha (EF-1a) gene, partial cds. Anathix ralla 37,319 16-Jul-97 rxa01095 857 GB_BA1:MTCY01B2 35938 Z95554 Mycobacterium tuberculosis H37Rv complete genome; segment 72/162. Mycobacterium tuberculosis 43,243 17-Jun-98 GB_HTG5:AC011632 175917 AC011632 Homo sapiens clone RP11-3N13, WORKING DRAFT SEQUENCE, 9 Homo sapiens 36,471 19-Nov-99 unordered pieces. GB_HTG5:AC011632 175917 AC011632 Homo sapiens clone RP11-3N13, WORKING DRAFT SEQUENCE, 9 Homo sapiens 36,836 19-Nov-99 unordered pieces. rxa01097 477 GB_BA2:AF030405 774 AF030405 Corynebacterium glutamicum cyclase (hisF) gene, complete cds. Corynebacterium glutamicum 100,000 13-Nov-97 GB_BA2:AF030405 774 AF030405 Corynebacterium glutamicum cyclase (hisF) gene, complete cds. Corynebacterium glutamicum 41,206 13-Nov-97 rxa01098 897 GB_BA2:AF030405 774 AF030405 Corynebacterium glutamicum cyclase (hisF) gene, complete cds. Corynebacterium glutamicum 97,933 13-Nov-97 GB_BA1:MSGY223 42061 AD000019 Mycobacterium tuberculosis sequence from clone y223. Mycobacterium tuberculosis 40,972 10-DEC-1996 GB_BA1:MLCB1610 40055 AL049913 Mycobacterium leprae cosmid B1610. Mycobacterium leprae 61,366 27-Aug-99 rxa01100 861 GB_BA2:AF051846 738 AF051846 Corynebacterium glutamicum phosphoribosylformimino-5-amino-1- Corynebacterium glutamicum 97,154 12-MAR-1998 phosphoribosyl-4- imidazolecarboxamide isomerase (hisA) gene, complete cds. GB_BA2:AF060558 636 AF060558 Corynebacterium glutamicum glutamine amidotransferase (hisH) gene, Corynebacterium glutamicum 95,455 29-Apr-98 complete cds. GB_HTG1:HSDJ140A9 221755 AL109917 Homo sapiens chromosome 1 clone RP1-140A9, *** SEQUENCING IN Homo sapiens 30,523 23-Nov-99 PROGRESS ***, in unordered pieces. rxa01101 756 GB_BA2:AF060558 636 AF060558 Corynebacterium glutamicum glutamine amidotransferase (hisH) gene, Corynebacterium glutamicum 94,462 29-Apr-98 complete cds. GB_BA1:SC4G6 36917 AL096884 Streptomyces coelicolor cosmid 4G6. Streptomyces coelicolor 38,378 23-Jul-99 A3 (2) GB_BA1:STMHISOPA 3981 M31628 S.coelicolor histidine biosynthesis operon encoding hisD, partial cds., and Streptomyces coelicolor 60,053 26-Apr-93 hisC, hisB, hisH, and hisA genes, complete cds. rxa01104 729 GB_BA1:STMHISOPA 3981 M31628 S. coelicolor histidine biosynthesis operon encoding hisD, partial cds., and Streptomyces coelicolor 58,333 26-Apr-93 hisC, hisB, hisH, and hisA genes, complete cds. GB_BA1:SC4G6 36917 AL096884 Streptomyces coelicolor cosmid 4G6. Streptomyces coelicolor 39,045 23-Jul-99 A3 (2) GB_BA1:MTCY336 32437 Z95586 Mycobacterium tuberculosis H37Rv complete genome, segment 70/162. Mycobacterium tuberculosis 60,364 24-Jun-99 rxa01105 1221 GB_BA1:MTCY336 32437 Z95586 Mycobacterium tuberculosis H37Rv complete genome; segment 70/162. Mycobacterium tuberculosis 60,931 24-Jun-99 GB_BA1:MSGY223 42061 AD000019 Mycobacterium tuberculosis sequence from clone y223. Mycobacterium tuberculosis 36,851 10-DEC-1996 GB_BA1:MLCB1610 40055 AL049913 Mycobacterium leprae cosmid B1610. Mycobacterium leprae 60,902 27-Aug-99 rxa01106 1449 GB_BA1:MSGY223 42061 AD000019 Mycobacterium tuberculosis sequence from clone y223. Mycobacterium tuberculosis 37,233 10-DEC-1996 GB_BA1:MSHISCD 2298 X65542 M. smegmatis genes hisD and hisC for histidinol dehydrogenase and histidinol- Mycobacterium smegmatis 60,111 30-Jun-93 phosphate aminotransferase, respectively. GB_BA1:MTCY336 32437 Z95586 Mycobacterium tuberculosis H37Rv complete genome; segment 70/162. Mycobacterium tuberculosis 58,420 24-Jun-99 rxa01145 1137 GB_BA1:CORAIA 4705 L09232 Corynebacterium glutamicum acetohydroxy acid synthase (ilvB) and (ilvN) Corynebacterium glutamicum 100,000 23-Feb-95 genes, and acetohydroxy acid isomeroreductase (ilvC) gene, complete cds. GB_BA1:BRLILVCA 1364 D14551 Brevibacterium flavum ilvC gene for acetohydroxy acid isomeroreductase, Corynebacterium glutamicum 99,560 3-Feb-99 complete cds. GB_PAT:E08232 1017 E08232 DNA encoding acetohydroxy-acid isomeroreductase. Corynebacterium glutamicum 99,803 29-Sep-97 rxa01162 1449 GB_PAT:A60299 2869 A60299 Sequence 18 from Patent WO9706261. Aspergillus niger 38,675 06-MAR-1998 GB_PR3:HS24E5 35506 Z82185 Human DNA sequence from Fosmid 24E5 on chromosome 22q11.2-qter Homo sapiens 36,204 23-Nov-99 contains parvalbumin, ESTs, STS. GB_PR3:AC005265 43900 AC005265 Homo sapiens chromosome 19, cosmid F19750, complete sequence. Homo sapiens 38,363 6-Jul-98 rxa01208 846 GB_HTG2:AC004965 323792 AC004965 Homo sapiens clone DJ1106H14, *** SEQUENCING IN PROGRESS ***, 42 Homo sapiens 36,058 12-Jun-98 unordered pieces. GB_HTG2:AC004965 323792 AC004965 Homo sapiens clone DJ1106H14, *** SEQUENCING IN PROGRESS ***, 42 Homo sapiens 36,058 12-Jun-98 unordered pieces. GB_PL2:TAU55859 2397 U55859 Triticum aestivum heat shock protein 80 mRNA, complete cds. Triticum aestivum 37,269 1-Feb-99 rxa01209 1528 GB_HTG3:AC011469 113436 AC011469 Homo sapiens chromosome 19 clone CIT-HSPC_475D23, *** SEQUENCING Homo sapiens 40,000 07-OCT-1999 IN PROGRESS ***, 31 unordered pieces. GB_HTG3:AC011469 113436 AC011469 Homo sapiens chromosome 19 clone CIT-HSPC_475D23, *** SEQUENCING Homo sapiens 40,000 07-OCT-1999 IN PROGRESS ***, 31 unordered pieces. GB_PL1:AB010077 77380 AB010077 Arabidopsis thaliana genomic DNA, chromosome 5, P1 clone: MYH19, Arabidopsis thaliana 36,803 20-Nov-99 complete sequence. rxa01215 1098 GB_BA1:MTCY10G2 38970 Z92539 Mycobacterium tuberculosis H37Rv complete genome; segment 47/162. Mycobacterium tuberculosis 37,047 17-Jun-98 GB_IN1:LEIPRPP 1887 M76553 Leishmania donovani phosphoribosylpyrophosphate synthetase gene, Leishmania donovani 50,738 7-Jun-93 complete cds. GB_HTG2:HSJ799D16 130149 AL050344 Homo sapiens chromosome 1 clone RP4-799D16 map p34.3-36.1, *** Homo sapiens 38,135 29-Nov-99 SEQUENCING IN PROGRESS ***, in unordered pieces. rxa01239 2556 GB_BA1:MTCY48 35377 Z74020 Mycobacterium tuberculosis H37Rv complete genome; segment 69/162. Mycobacterium tuberculosis 38,139 17-Jun-98 GB_PR2:AB029032 6377 AB029032 Homo sapiens mRNA for KIAA1109 protein, partial cds. Homo sapiens 39,394 4-Aug-99 GB_GSS9:AQ107201 355 AQ107201 HS_3098_A1_C03_T7 CIT Approved Human Genomic Sperm Library D Homo Homo sapiens 41,408 28-Aug-98 sapiens genomic clone Plate = 3098 Col = 5 Row = E, genomic survey sequence. rxa01253 873 GB_PL2:F5O8 99923 AC005990 Arabidopsis thaliana chromosome 1 BAC F5O8 sequence, complete Arabidopsis thaliana 36,118 23-DEC-1998 sequence. GB_PL2:F5O8 99923 AC005990 Arabidopsis thaliana chromosome 1 BAC F5O8 sequence, complete Arabidopsis thaliana 35,574 23-DEC-1998 sequence. GB_IN1:CELC06G1 31205 U41014 Caenorhabditis elegans cosmid C06G1. Caenorhabditis elegans 38,560 30-Nov-95 rxa01321 1044 GB_GSS14:AQ518843 441 AQ518843 HS_5106_A1_D10_SP6E RPCI-11 Human Male BAC Library Homo sapiens Homo sapiens 41,121 05-MAY-1999 genomic clone Plate = 682 Col = 19 Row = G, genomic survey sequence GB_HTG2:AC007473 194859 AC007473 Drosophila melanogaster chromosome 2 clone BACR38D12 (D590) RPCI-98 Drosophila melanogaster 40,634 2-Aug-99 38.D.12 map 48A-48B strain y; cn bw sp, *** SEQUENCING IN PROGRESS ***, 60 unordered pieces. GB_HTG4:AC011696 115847 AC011696 Drosophila melanogaster chromosome 2 clone BACR35F01 (D1156) RPCI-98 Drosophila melanogaster 38,290 26-OCT-1999 35.F.1 map 48A-48C strain y; cn bw sp, *** SEQUENCING IN PROGRESS ***, 108 unordered pieces. rxa01352 706 GB_PL2:ATAC005167 83260 AC005167 Arabidopsis thaliana chromosome II BAC F12A24 genomic sequence, Arabidopsis thaliana 34,311 15-OCT-1998 complete sequence. GB_PL2:ATAC005825 97380 AC005825 Arabidopsis thaliana chromosome II BAC T24121 genomic sequence, complete Arabidopsis thaliana 34,311 12-Apr-99 sequence. GB_HTG3:AC011150 127222 AC011150 Homo sapiens clone 4_K_17, LOW-PASS SEQUENCE SAMPLING. Homo sapiens 37,722 01-OCT-1999 rxa01360 259 GB_EST32:AI725583 728 AI725583 BNLGHi12371 Six-day Cotton fiberGossypium hirsutum cDNA 5′ similar to Gossypium hirsutum 38,492 11-Jun-99 (U86081) root hair defective 3 [Arabidopsis thaliana], mRNA sequence. GB_PR2:HS227P17 82951 Z81007 Human DNA sequence from PAC 227P17, between markers DXS6791 Homo sapiens 39,738 23-Nov-99 andDXS8038 on chromosome X contains CpG island, EST. GB_EST34:AV171099 173 AV171099 AV171099 Mus musculus head C57BL/6J 14, 17 day embryo Mus musculus Mus musculus 46,237 6-Jul-99 cDNA clone 3200002M11, mRNA sequence. rxa01361 629 GB_RO:AB008915S1 530 AB008915 Mus musculus mGpi1 gene, exon 1. Mus musculus 45,574 28-Sep-99 GB_EST22:AI050532 293 AI050532 uc83d10.y1 Sugano mouse kidney mkia Mus musculus cDNA clone Mus musculus 44,097 9-Jul-98 IMAGE:1432243 5′ similar to TR:O35120 O35120 MGPI1P.;, mRNA sequence. GB_RO:AB008895 3062 AB008895 Mus musculus mRNA for mGpi1p, complete cds. Mus musculus 41,316 23-Nov-97 rxa01381 944 GB_PL1:AB005237 87835 AB005237 Arabidopsis thaliana genomic DNA, chromosome 5, P1 clone: MJJ3, complete Arabidopsis thaliana 36,606 20-Nov-99 sequence. GB_GSS5:AQ766840 491 AQ766840 HS_2026_A2_C09_T7C CIT Approved Human Genomic Sperm Library D Homo sapiens 37,916 28-Jul-99 Homo sapiens genomic clone Plate = 2026 Col = 18 Row = E, genomic survey sequence. GB_BA1:MTV043 68848 AL022004 Mycobacterium tuberculosis H37Rv complete genome; segment 40/162. Mycobacterium tuberculosis 37,419 24-Jun-99 rxa01393 993 GB_BA1:CGLYSEG 2374 X96471 C. glutamicum lysE and lysG genes. Corynebacterium glutamicum 34,831 24-Feb-97 GB_BA1:SC5A7 40337 AL031107 Streptomyces coelicolor cosmid 5A7. Streptomyces coelicolor 35,138 27-Jul-98 GB_PR3:AC004054 112184 AC004054 Homo sapiens chromosome 4 clone B220G8 map 4q21, complete sequence. Homo sapiens 37,277 9-Jul-98 rxa01394 822 GB_BA1:CGLYSEG 2374 X96471 C. glutamicum lysE and lysG genes. Corynebacterium glutamicum 100,000 24-Feb-97 GB_GSS5:AQ769223 500 AQ769223 HS_3155_B2_G10_T7C CIT Approved Human Genomic Sperm Library D Homo sapiens 38,400 28-Jul-99 Homo sapiens genomic clone Plate = 3155 Col = 20 Row = N, genomic survey sequence. GB_BA1:CGLYSEG 2374 X96471 C. glutamicum lysE and lysG genes. Corynebacterium glutamicum 33,665 24-Feb-97 rxa01416 630 GB_BA1:SC3C3 31382 AL031231 Streptomyces coelicolor cosmid 3C3. Streptomyces coelicolor 62,726 10-Aug-98 GB_BA1:MLCB22 40281 Z98741 Mycobacterium leprae cosmid B22. Mycobacterium leprae 39,159 22-Aug-97 GB_BA1:MTV002 56414 AL008967 Mycobacterium tuberculosis H37Rv complete genome; segment 122/162. Mycobacterium tuberculosis 37,340 17-Jun-98 rxa01442 1347 GB_BA1:D90827 18886 D90827 E. coli genomic DNA, Kohara clone #336 (41.2-41.6 min). Escherichia coli 58,517 21-MAR-1997 GB_BA1:D90828 14590 D90828 E. coli genomic DNA, Kohara clone #336gap (41.6-41.9 min.). Escherichia coli 56,151 21-MAR-1997 GB_BA2:AE000279 10855 AE000279 Escherichia coli K-12 MG1655 section 169 of 400 of the complete genome. Escherichia coli 56,021 12-Nov-98 rxa01446 1413 GB_BA1:SCH10 39524 AL049754 Streptomyces coelicolor cosmid H10. Streptomyces coelicolor 39,037 04-MAY-1999 GB_BA1:MTY13E10 35019 Z95324 Mycobacterium tuberculosis H37Rv complete genome; segment 18/162. Mycobacterium tuberculosis 40,130 17-Jun-98 GB_BA1:MLCB4 36310 AL023514 Mycobacterium leprae cosmid B4. Mycobacterium leprae 37,752 27-Aug-99 rxa01483 1395 GB_BA1:MTCY98 31225 Z83860 Mycobacterium tuberculosis H37Rv complete genome; segment 103/162. Mycobacterium tuberculosis 39,057 17-Jun-98 GB_BA1:MSGB1229CS 30670 L78812 Mycobacterium leprae cosmid B1229 DNA sequence. Mycobacterium leprae 54,382 15-Jun-96 GB_BA2:AF027507 5168 AF027507 Mycobacterium smegmatis dGTPase (dgt), and primase (dnaG) genes, Mycobacterium smegmatis 52,941 16-Jan-98 complete cds; tRNA-Asn gene, complete sequence. rxa01486 757 GB_BA1:MTV002 56414 AL008967 Mycobacterium tuberculosis H37Rv complete genome; segment 122/162. Mycobacterium tuberculosis 40,941 17-Jun-98 GB_BA1:MLCB22 40281 Z98741 Mycobacterium leprae cosmid B22. Mycobacterium leprae 38,451 22-Aug-97 GB_BA1:SC3C3 31382 AL031231 Streptomyces coelicolor cosmid 3C3. Streptomyces coelicolor 61,194 10-Aug-98 rxa01489 1146 GB_BA1:CORFADS 1547 D37967 Corynebacterium ammoniagenes gene for FAD synthetase, complete cds Corynebacterium 58,021 8-Feb-99 ammoniagenes GB_BA1:MLCB22 40281 Z98741 Mycobacterium leprae cosmid B22. Mycobacterium leprae 38,414 22-Aug-97 GB_BA1:SC10A7 39739 AL078618 Streptomyces coelicolor cosmid 10A7. Streptomyces coelicolor 36,930 9-Jun-99 rxa01491 774 GB_BA1:MTV002 56414 AL008967 Mycobacterium tuberculosis H37Rv complete genome; segment 122/162. Mycobacterium tuberculosis 37,062 17-Jun-98 GB_EST13:AA356956 255 AA356956 EST65614 Jurkat T-cells III Homo sapiens cDNA 5′ end, mRNA sequence. Homo sapiens 37,647 21-Apr-97 GB_OV:OMDNAPROI 7327 X92380 O. mossambicus prolactin I gene. Tilapia mossambica 38,289 19-OCT-1995 rxa01508 1662 GB_IN1:CEF28C12 14653 Z93380 Caenorhabditis elegans cosmid F28C12, complete sequence. Caenorhabditis elegans 37,984 23-Nov-98 GB_IN1:CEF28C12 14653 Z93380 Caenorhabditis elegans cosmid F28C12, complete sequence. Caenorhabditis elegans 38,469 23-Nov-98 rxa01512 723 GB_BA1:SCE9 37730 AL049841 Streptomyces coelicolor cosmid E9. Streptomyces coelicolor 39,021 19-MAY-1999 GB_BA1:MAU88875 840 U88875 Mycobacterium avium hypoxanthine-guanine phosphoribosyl transferase gene, Mycobacterium avium 57,521 05-MAR-1997 complete cds. GB_BA1:MTY15C10 33050 Z95436 Mycobacterium tuberculosis H37Rv complete genome; segment 154/162. Mycobacterium tuberculosis 40,086 17-Jun-98 rxa01514 711 GB_BA1:MTCY7H7B 24244 Z95557 Mycobacterium tuberculosis H37Rv complete genome; segment 153/162. Mycobacterium tuberculosis 43,343 18-Jun-98 GB_BA1:MLCB2548 38916 AL023093 Mycobacterium leprae cosmid B2548. Mycobacterium leprae 38,177 27-Aug-99 GB_PL1:EGGTPCHI 242 Z49757 E. gracilis mRNA for GTP cyclohydrolase I (core region). Euglena gracilis 64,876 20-OCT-1995 rxa01515 975 GB_BA1:ECOUW93 338534 U14003 Escherichia coli K-12 chromosomal region from 92.8 to 00.1 minutes. Escherichia coli 38,943 17-Apr-96 GB_BA1:ECOUW93 338534 U14003 Escherichia coli K-12 chromosomal region from 92.8 to 00.1 minutes. Escherichia coli 37,500 17-Apr-96 GB_BA1:MTCY49 39430 Z73966 Mycobacterium tuberculosis H37Rv complete genome; segment 93/162. Mycobacterium tuberculosis 38,010 24-Jun-99 rxa01516 513 GB_IN1:DME238847 5419 AJ238847 Drosophila melanogaster mRNA for drosophila dodeca-satellite protein 1 (DDP- Drosophila melanogaster 36,346 13-Aug-99 1). GB_HTG3:AC009210 103814 AC009210 Drosophila melanogaster chromosome 2 clone BACR01I06 (D1054) RPCI-98 Drosophila melanogaster 37,897 20-Aug-99 01.I.6 map 55D-55D strain y; cn bw sp, *** SEQUENCING IN PROGRESS ***, 86 unordered pieces. GB_IN2:AF132179 4842 AF132179 Drosophila melanogaster clone LD21677 unknown mRNA. Drosophila melanogaster 36,149 3-Jun-99 rxa01517 600 GB_PL2:F6H8 82596 AF178045 Arabidopsis thaliana BAC F6H8. Arabidopsis thaliana 35,846 19-Aug-99 GB_PL2:AF038831 647 AF038831 Sorosporium saponariae internal transcribed spacer 1, 5.8S ribosomal RNA Sorosporium saponariae 40,566 13-Apr-99 gene; and internal transcribed spacer 2, complete sequence. GB_PL2:ATAC005957 108355 AC005957 Arabidopsis thaliana chromosome II BAC T15J14 genomic sequence, Arabidopsis thaliana 38,095 7-Jan-99 complete sequence. rxa01521 921 GB_BA1:ANANIFBH 5936 J05111 Anabaena sp. (clone AnH20.1) nitrogen fixation operon nifB, fdxN, nifS, nifU, Anabaena sp. 38,206 26-Apr-93 and nifH genes, complete cds. GB_PR2:AC002461 197273 AC002461 Human BAC clone RG204I16 from 7q31, complete sequence. Homo sapiens 36,623 20-Aug-97 GB_PR2:AC002461 197273 AC002461 Human BAC clone RG204I16 from 7q31, complete sequence. Homo sapiens 34,719 20-Aug-97 rxa01528 651 GB_RO:MM437P9 165901 AL049866 Mus musculus chromosome X, clone 437P9. Mus musculus 37,500 29-Jun-99 GB_PR3:AC005740 186780 AC005740 Homo sapiens chromosome 5p, BAC clone 50g21 (LBNL H154), complete Homo sapiens 37,031 01-OCT-1998 sequence. GB_PR3:AC005740 186780 AC005740 Homo sapiens chromosome 5p, BAC clone 50g21 (LBNL H154), complete Homo sapiens 38,035 01-OCT-1998 sequence. rxa01551 1998 GB_BA1:MTCY22G10 35420 Z84724 Mycobacterium tuberculosis H37Rv complete genome; segment 21/162. Mycobacterium tuberculosis 38,371 17-Jun-98 GB_BA2:ECOUW89 176195 U00006 E. coli chromosomal region from 89.2 to 92.8 minutes. Escherichia coli 38,064 17-DEC-1993 GB_BA1:SCQ11 15441 AL096823 Streptomyces coelicolor cosmid Q11. Streptomyces coelicolor 60,775 8-Jul-99 rxa01561 1053 GB_IN1:CEY62H9A 47396 AL032630 Caenorhabditis elegans cosmid Y62H9A, complete sequence. caenorhabditis elegans 38,514 2-Sep-99 GB_PR4:HSU51003 3202 U51003 Homo sapiens DLX-2 (DLX-2) gene, complete cds. Homo sapiens 37,730 07-DEC-1999 GB_OM:PIGDAO1 395 M18444 Pig D-amino acid oxidase (DAO) gene, exon 1. Sus scrofa 39,340 27-Apr-93 rxa01599 1785 GB_BA1:MTCI125 37432 Z98268 Mycobacterium tuberculosis H37Rv complete genome; segment 76/162. Mycobacterium tuberculosis 63,300 17-Jun-98 GB_BA1:U00021 39193 U00021 Mycobacterium leprae cosmid L247. Mycobacterium leprae 36,756 29-Sep-94 GB_BA1:MLCB1351 38936 Z95117 Mycobacterium leprae cosmid B1351. Mycobacterium leprae 36,756 24-Jun-97 rxa01617 795 GB_PR2:HSMTM0 217657 AL034384 Human chromosome Xq28, cosmid clones 7H3, 14D7, C1230, 11E7, F1096 Homo sapiens 40,811 5-Jul-99 A12197, 12G8, A09100; complete sequence bases 1..217657. GB_PR2:HS13D10 153147 AL021407 Homo sapiens DNA sequence from PAC 13D10 on chromosome 6p22.3-23. Homo sapiens 38,768 23-Nov-99 Contains CpG island. GB_PR2:HSMTM0 217657 AL034384 Human chromosome Xq28, cosmid clones 7H3, 14D7, C1230, 11E7, F1096, Homo sapiens 39,018 5-Jul-99 A12197, 12G8, A09100; complete sequence bases 1..217657. rxa01657 723 GB_BA1:MTCY1A10 25949 Z95387 Mycobacterium tuberculosis H37Rv complete genome; segment 117/162. Mycobacterium tuberculosis 40,656 17-Jun-98 GB_EST6:D79278 392 D79278 HUM213D06B Human aorta polyA + (TFujiwara) Homo sapiens cDNA clone Homo sapiens 44,262 9-Feb-96 GEN-213D06 5′, mRNA sequence. GB_BA2:AF129925 10243 AF129925 Thiobacillus ferrooxidans carboxysome operon, complete cds. Thiobacillus ferrooxidans 40,709 17-MAY-1999 rxa01660 675 GB_BA1:MTV013 11364 AL021309 Mycobacterium tuberculosis H37Rv complete genome; segment 134/162. Mycobacterium tuberculosis 40,986 17-Jun-98 GB_RO:MMFV1 6480 X97719 M. musculus retrovirus restriction gene Fv1. Mus musculus 35,364 29-Aug-96 GB_PAT:A67508 6480 A67508 Sequence 1 from Patent WO9743410. Mus musculus 35,364 05-MAY-1999 rxa01678 651 GB_VI:TVU95309 600 U95309 Tula virus O64 nucleocapsid protein gene, partial cds. Tula virus 41,894 28-OCT-1997 GB_VI:TVU95303 600 U95303 Tula virus O52 nucleocapsid protein gene, partial cds. Tula virus 41,712 28-OCT-1997 GB_VI:TVU95302 600 U95302 Tula virus O24 nucleocapsid protein gene, partial cds. Tula virus 39,576 28-OCT-1997 rxa01679 1359 GB_EST5:H91843 362 H91843 ys81e01.s1 Soares retina N2b4HR Homo sapiens cDNA clone IMAGE:221208 Homo sapiens 39,157 29-Nov-95 3′ similar to gb:X63749_rna1 GUANINE NUCLEOTIDE-BINDING PROTEIN G (T), ALPHA-1 (HUMAN);, mRNA sequence GB_STS:G26925 362 G26925 human STS SHGC-30023, sequence tagged site. Homo sapiens 39,157 14-Jun-96 GB_PL2:AF139451 1202 AF139451 Gossypium robinsonii CelA2 pseudogene, partial sequence. Gossypium robinsonii 38,910 1-Jun-99 rxa01690 1224 GB_BA1:SC1C2 42210 AL031124 Streptomyces coelicolor cosmid 1C2. Streptomyces coelicolor 60,644 15-Jan-99 GB_EST22:AI064232 493 AI064232 GH04563.5prime GH Drosophila melanogaster head pOT2 Drosophila Drosophila melanogaster 38,037 24-Nov-98 melanogaster cDNA clone GH04563 5prime, mRNA sequence. GB_IN2:AF117896 1020 AF117896 Drosophila melanogaster neuropeptide F (npf) gene, complete cds. Drosophila melanogaster 36,122 2-Jul-99 rxa01692 873 GB_BA2:AF067123 1034 AF067123 Lactobacillus reuteri cobalamin biosynthesis protein J (cbiJ) gene, partial cds, Lactobacillus reuteri 48,079 3-Jun-98 and uroporphyrin-III C-methyltransferase (sumT) gene, complete cds. GB_RO:RATNFHPEP 3085 M37227 Rat heavy neurofilament (NF-H) polypeptide, partial cds. Rattus norvegicus 37,093 27-Apr-93 GB_RO:RSNFH 3085 X13804 Rat mRNA for heavy neurofilament polypeptide NF-H C-terminus. Rattus sp. 37,093 14-Jul-95 rxa01698 1353 GB_BA2:AF124600 4115 AF124600 Corynebacterium glutamicum chorismate synthase (aroC), shikimate kinase Corynebacterium glutamicum 100,000 04-MAY-1999 (arok), and 3-dehydroquinate synthase (aroB) genes, complete cds; and putative cytoplasmic peptidase (pepQ) gene, partial cds. GB_BA1:MTCY159 33818 Z83863 Mycobacterium tuberculosis H37Rv complete genome; segment 111/162. Mycobacterium tuberculosis 36,323 17-Jun-98 GB_BA1:MSGB937CS 38914 L78820 Mycobacterium leprae cosmid B937 DNA sequence. Mycobacterium leprae 62,780 15-Jun-96 rxa01699 693 GB_BA2:AF124600 4115 AF124600 Corynebacterium glutamicum chorismate synthase (aroC), shikimate kinase Corynebacterium glutamicum 100,000 04-MAY-1999 (aroK), and 3-dehydroquinate synthase (aroB) genes, complete cds; and putative cytoplasmic peptidase (pepQ) gene, partial cds. GB_BA2:AF016585 41097 AF016585 Streptomyces caelestis cytochrome P-450 hydroxylase homolog (nidi) gene, Streptomyces caelestis 40,260 07-DEC-1997 partial cds; polyketide synthase modules 1 through 7 (nidA) genes, complete cds; and N-methyltransferase homolog gene, partial cds. GB_EST9:C19712 399 C19712 C19712 Rice panicle at ripening stage Oryza sativa cDNA clone E10821_1A, Oryza sativa 45,425 24-OCT-1996 mRNA sequence. rxa01712 805 GB_EST21:AA952466 278 AA952466 TENS1404 T. cruzi epimastigote normalized cDNA Library Trypanosoma cruzi Trypanosoma cruzi 40,876 29-OCT-1998 cDNA clone 1404 5′, mRNA sequence GB_EST21:AA952466 278 AA952466 TENS1404 T. cruzi epimastigote normalized cDNA Library Trypanosoma cruzi Trypanosoma cruzi 41,367 29-OCT-1998 cDNA clone 1404 5′, mRNA sequence. rxa01719 684 GB_HTG1:HSDJ534K7 154416 AL109925 Homo sapiens chromosome 1 clone RP4-534K7, *** SEQUENCING IN Homo sapiens 35,651 23-Nov-99 PROGRESS ***, in unordered pieces. GB_HTG1:HSDJ534K7 154416 AL109925 Homo sapiens chromosome 1 clone RP4-534K7, *** SEQUENCING IN Homo sapiens 35,651 23-Nov-99 PROGRESS ***, in unordered pieces. GB_EST27:AI447108 431 AI447108 mq91e08x1 Stratagene mouse heart (#937316) Mus musculus cDNA clone Mus musculus 39,671 09-MAR-1999 IMAGE:586118 3′, mRNA sequence. rxa01720 1332 GB_PR4:AC006322 179640 AC006322 Homo sapiens PAC clone DJ1060B11 from 7q11.23-q21.1, complete Homo sapiens 35,817 18-MAR-1999 sequence. GB_PL2:TM018A10 106184 AF013294 Arabidopsis thaliana BAC TM018A10. Arabidopsis thaliana 35,698 12-Jul-97 GB_PR4:AC006322 179640 AC006322 Homo sapiens PAC clone DJ1060B11 from 7q11.23-q21.1, complete Homo sapiens 37,243 18-MAR-1999 sequence. rxa01746 876 GB_EST3:R46227 443 R46227 yg52a03.s1 Soares infant brain 1NIB Homo sapiens cDNA clone Homo sapiens 42,812 22-MAY-1995 IMAGE:36000 3′, mRNA sequence. GB_EST3:R46227 443 R46227 yg52a03.s1 Soares infant brain 1NIB Homo sapiens cDNA clone Homo sapiens 42,655 22-MAY-1995 IMAGE:36000 3′, mRNA sequence. rxa01747 1167 GB_BA1:MTCY190 34150 Z70283 Mycobacterium tuberculosis H37Rv complete genome; segment 98/162. Mycobacterium tuberculosis 59,294 17-Jun-98 GB_BA1:MLCB22 40281 Z98741 Mycobacterium leprae cosmid B22. Mycobacterium leprae 57,584 22-Aug-97 GB_BA1:SC5F7 40024 AL096872 Streptomyces coelicolor cosmid 5F7. Streptomyces coelicolor 61,810 22-Jul-99 A3 (2) rxa01757 924 GB_EST21:AA918454 416 AA918454 om38c02.s1 Soares_NFL_T_GBC_S1 Homo sapiens cDNA clone Homo sapiens 39,655 23-Jun-98 IMAGE:1543298 3′ similar to WP:F28F8.3 CE09757 SMALL NUCLEAR RIBONUCLEOPROTEIN E;, mRNA sequence. GB_EST4:H34042 345 H34042 EST110563 Rat PC-12 cells, NGF-treated (9 days) Rattus sp. cDNA clone Rattus sp. 35,942 2-Apr-98 RPNBI81 5′ end, mRNA sequence. GB_EST20:AA899038 450 AA899038 NCP6G8T7 Perithecial Neurospora crassa cDNA clone NP6G8 3′ end, mRNA Neurospora crassa 40,000 12-Apr-98 sequence. rxa01807 915 GB_BA1:AP000063 185300 AP000063 Aeropyrum pernix genomic DNA, section 6/7. Aeropyrum pernix 40,067 22-Jun-99 GB_HTG4:AC010694 115857 AC010694 Drosophila melanogaster clone RPCI98-6H2, *** SEQUENCING IN Drosophila melanogaster 35,450 16-OCT-1999 PROGRESS ***, 75 unordered pieces. GB_HTG4:AC010694 115857 AC010694 Drosophila melanogaster clone RPCI98-6H2, *** SEQUENCING IN Drosophila melanogaster 35,450 16-OCT-1999 PROGRESS ***, 75 unordered pieces. rxa01821 401 GB_BA1:CGL007732 4460 AJ007732 Corynebacterium glutamicum 3′ ppc gene, secG gene, amt gene, ocd gene Corynebacterium glutamicum 100,000 7-Jan-99 and 5′ soxA gene. GB_RO:RATALGL 7601 M24108 Rattus norvegicus (clone A2U42) alpha2u globulin gene, exons 1-7. Rattus norvegicus 38,692 15-DEC-1994 GB_OV:APIGY2 1381 X78272 Anas platyrhynchos (Super M) IgY upsilon heavy chain gene, exon 2. Anas platyrhynchos 36,962 15-Feb-99 rxa01835 654 GB_EST30:AI629479 353 AI629479 486101D10.x1 486 - leaf primordia cDNA library from Hake lab Zea mays Zea mays 38,109 26-Apr-99 cDNA, mRNA sequence. GB_STS:G48245 515 G48245 SHGC-62915 Human Homo sapiens STS genomic, sequence tagged site. Homo sapiens 37,021 26-MAR-1999 GB_GSS3:B49052 515 B49052 RPCI11-4I12.TV RPCI-11 Homo sapiens genomic clone RPCI-11-4I12, Homo sapiens 37,021 8-Apr-99 genomic survey sequence. rxa01850 1470 GB_BA2:ECOUW67_0 110000 U18997 Escherichia coli K-12 chromosomal region from 67.4 to 76.0 minutes. Escherichia coli 37,196 U18997 GB_BA2:AE000392 10345 AE000392 Escherichia coil K-12 MG1655 section 282 of 400 of the complete genome. Escherichia coli 38,021 12-Nov-98 GB_BA2:U32715 13136 U32715 Haemophilus influenzae Rd section 30 of 163 of the complete genome. Haemophilus influenzae Rd 39,860 29-MAY-1998 rxa01878 1002 GB_HTG1:CEY64F11 177748 Z99776 Caenorhabditis elegans chromosome IV clone Y64F11, *** SEQUENCING IN Caenorhabditis elegans 37,564 14-OCT-1998 PROGRESS ***, in unordered pieces. GB_HTG1:CEY64F11 177748 Z99776 Caenorhabditis elegans chromosome IV clone Y64F11, *** SEQUENCING IN Caenorhabditis elegans 37,564 14-OCT-1998 PROGRESS ***, in unordered pieces. GB_HTG1:CEY64F11 177748 Z99776 Caenorhabditis elegans chromosome IV clone Y64F11, *** SEQUENCING IN Caenorhabditis elegans 37,576 14-OCT-1998 PROGRESS ***, in unordered pieces. rxa01892 852 GB_BA1:MTCY274 39991 Z74024 Mycobacterium tuberculosis H37Rv complete genome; segment 126/162. Mycobacterium tuberculosis 35,910 19-Jun-98 GB_BA1:MLCB250 40603 Z97369 Mycobacterium leprae cosmid B250. Mycobacterium leprae 64,260 27-Aug-99 GB_BA1:MSGB1529CS 36985 L78824 Mycobacterium leprae cosmid B1529 DNA sequence. Mycobacterium leprae 64,260 15-Jun-96 rxa01894 978 GB_BA1:MTCY274 39991 Z74024 Mycobacterium tuberculosis H37Rv complete genome; segment 126/162. Mycobacterium tuberculosis 37,229 19-Jun-98 GB_IN1:CELF46H5 38886 U41543 Caenorhabditis elegans cosmid F46H5. Caenorhabditis elegans 38,525 29-Nov-96 GB_HTG3:AC009204 115633 AC009204 Drosophila melanogaster chromosome 2 clone BACR03E19 (D1033) RPCI-98 Drosophila melanogaster 31,579 18-Aug-99 03.E.19 map 36E-37C strain y; cn bw sp, *** SEQUENCING IN PROGRESS ***, 94 unordered pieces. rxa01920 1125 GB_BA2:AF112536 1798 AF112536 Corynebacterium glutamicum ribonucleotide reductase beta-chain (nrdF) Corynebacterium glutamicum 99.733 5-Aug-99 gene, complete cds. GB_BA1:CANRDFGEN 6054 Y09572 Corynebacterium ammoniagenes nrdH, nrdI, nrdE, nrdF genes. Corynebacterium 70,321 18-Apr-98 ammoniagenes GB_BA2:AF050168 1228 AF050168 Corynebacterium ammoniagenes ribonucleoside diphosphate reductase small Corynebacterium 72,082 23-Apr-98 subunit (nrdF) gene, complete cds. ammoniagenes rxa01928 960 GB_BA1:CGPAN 2164 X96580 C. glutamicum panB, panC & xylB genes. Corynebacterium glutamicum 100,000 11-MAY-1999 GB_PL1:AP000423 154478 AP000423 Arabidopsis thaliana chloroplast genomic DNA, complete sequence, Chloroplast Arabidopsis 35,917 15-Sep-99 strain:Columbia. thaliana GB_PL1:AP000423 154478 AP000423 Arabidopsis thaliana chloroplast genomic DNA, complete sequence, Chloroplast Arabidopsis 33,925 15-Sep-99 strain:Columbia. thaliana rxa01929 936 GB_BA1:CGPAN 2164 X96580 C. glutamicum panB, panC & xylB genes. Corynebacterium glutamicum 100,000 11-MAY-1999 GB_BA1:XCU33548 8429 U33548 Xanthomonas campestris hrpB pathogenicity locus proteins HrpB1, HrpB2, Xanthomonas campestris pv. 38,749 19-Sep-96 HrpB3, HrpB4, HrpB5, HrpB6, HrpB7, HrpB8, HrpA1, and ORF62 vesicatoria genes, complete cds. GB_BA1:XANHRPB6A 1329 M99174 Xanthomonas campestris hrpB6 gene, complete cds. Xanthomonas campestris 39,305 14-Sep-93 rxa01940 1059 GB_IN2:CFU43371 1060 U43371 Crithidia fasciculata inosine-uridine preferring nucleoside hydrolase (IUNH) Crithidia fasciculata 61,417 18-Jun-96 gene, complete cds. GB_BA2:AE001467 11601 AE001467 Helicobacter pylori, strain J99 section 28 of 132 of the complete genome Helicobacter pylori J99 38,560 20-Jan-99 GB_RO:AF175967 3492 AF175967 Homo sapiens Leman coiled-coil protein (LCCP) mRNA, complete cds. Mus musculus 40,275 26-Sep-99 rxa02022 1230 GB_BA1:CGDAPE 1966 X81379 C. glutamicum dapE gene and orf2. Corynebacterium glutamicum 100,000 8-Aug-95 GB_BA1:CGDNAAROP 2612 X85965 C. glutamicum ORF3 and aroP gene. Corynebacterium glutamicum 38,889 30-Nov-97 GB_BA1:APU47055 6469 U47055 Anabaena PCC7120 nitrogen fixation proteins (nifE, nifN, nifX, nifW) genes, Anabaena PCC7120 36,647 17-Feb-96 complete cds, and nitrogenase (nifK) and hesA genes, partial cds. rxa02024 859 GB_BA1:MTCI364 29540 Z93777 Mycobacterium tuberculosis H37Rv complete genome, segment 52/162. Mycobacterium tuberculosis 59,415 17-Jun-98 GB_BA1:MSGB1912CS 38503 L01536 M. leprae genomic dna sequence, cosmid b1912. Mycobacterium leprae 57,093 14-Jun-96 GB_BA1:MLU15180 38675 U15180 Mycobacterium leprae cosmid B1756. Mycobacterium leprae 57,210 09-MAR-1995 rxa02027 rxa02031 rxa02072 1464 GB_BA1:CGGDHA 2037 X72855 C. glutamicum GDHA gene. Corynebacterium glutamicum 99,317 24-MAY-1993 GB_BA1:CGGDH 2037 X59404 Corynebacterium glutamicum, gdh gen for glutamate dehydrogenase. Corynebacterium glutamicum 94,387 30-Jul-99 GB_BA1:PAE18494 1628 Y18494 Pseudomonas aeruginosa gdhA gene, strain PAC1. Pseudomonas aeruginosa 62,247 6-Feb-99 rxa02085 2358 GB_BA1:MTCY22G8 22550 Z95585 Mycobacterium tuberculosis H37Rv complete genome; segment 49/162. Mycobacterium tuberculosis 38,442 17-Jun-98 GB_BA1:MLCB33 42224 Z94723 Mycobacterium leprae cosmid B33. Mycobacterium leprae 56,486 24-Jun-97 GB_BA1:ECOUW85 91414 M87049 E. coli genomic sequence of the region from 84.5 to 86.5 minutes. Escherichia coli 52,127 29-MAY-1995 rxa02093 927 GB_EST14:AA448146 452 AA448146 zw82h01.r1 Soares_testis_NHT Homo sapiens cDNA clone IMAGE.782737 5′, Homo sapiens 34,163 4-Jun-97 mRNA sequence. GB_EST17:AA641937 444 AA641937 ns18b10.r1 NCI_CGAP_GCB1 Homo sapiens cDNA clone IMAGE:1183963 5′, Homo sapiens 35,586 27-OCT-1997 mRNA sequence. GB_PR3:AC003074 143029 AC003074 Human PAC clone DJ0596O09 from 7p15, complete sequence. Homo sapiens 31,917 6-Nov-97 rxa02106 1179 GB_BA1:SC1A6 37620 AL023496 Streptomyces coelicolor cosmid 1A6. Streptomyces coelicolor 35,818 13-Jan-99 GB_PR4:AC005553 179651 AC005553 Homo sapiens chromosome 17, clone hRPK. 112_J_9, complete sequence. Homo sapiens 34,274 31-DEC-1998 GB_EST3:R49746 397 R49746 yg71g10.r1 Soares infant brain 1NIB Home sapiens cDNA clone Homo sapiens 41,162 18-MAY-1995 IMAGE:38768 5′ similar to gb:V00567 BETA-2-MICROGLOBULIN PRECURSOR (HUMAN);, mRNA sequence. rxa02111 1407 GB_BA1:SC6G10 36734 AL049497 Streptomyces coelicolor cosmid 6G10. Streptomyces coelicolor 50,791 24-MAR-1999 GB_BA1:U00010 41171 U00010 Mycobacterium leprae cosmid B1170. Mycobacterium leprae 37,563 01-MAR-1994 GB_BA1:MTCY336 32437 Z95586 Mycobacterium tuberculosis H37Rv complete genome; segment 70/162. Mycobacterium tuberculosis 39,504 24-Jun-99 rxa02112 960 GB_HTG3:AC010579 157658 AC010579 Drosophila melanogaster chromosome 3 clone BACR09D08 (D1101) RPCI-98 Drosophila melanogaster 37,909 24-Sep-99 09.D.8 map 96F-96F strain y; cn bw sp, *** SEQUENCING IN PROGRESS ***, 121 unordered pieces. GB_GSS3:B09839 1191 B09839 T12A12-Sp6 TAMU Arabidopsis thaliana genomic clone T12A12, genomic Arabidopsis thaliana 37,843 14-MAY-1997 survey sequence. GB_HTG3:AC010579 157658 AC010579 Drosophila melanogaster chromosome 3 clone BACR09D08 (D1101) RPCI-98 Drosophila melanogaster 37,909 24-Sep-99 09.D.8 map 96F-96F strain y; cn bw sp, *** SEQUENCING IN PROGRESS ***, 121 unordered pieces. rxa02134 1044 GB_BA1:SCSECYDNA 6154 X83011 S. coelicolor secY locus DNA. Streptomyces coelicolor 36,533 02-MAR-1998 GB_EST32:AI731596 568 AI731596 BNLGHi10185 Six-day Cotton fiber Gossypium hirsutum cDNA 5′ similar to Gossypium hirsutum 33,451 11-Jun-99 (AC004005) putative ribosomal protein L7 [Arabidopsis thaliana], mRNA sequence. GB_BA1:SCSECYDNA 6154 X83011 S. coelicolor secY locus DNA. Streptomyces coelicolor 36,756 02-MAR-1998 rxa02135 1197 GB_PR3:HS525L6 168111 AL023807 Human DNA sequence from clone RP3-525L6 on chromosome 6p22.3-23 Homo sapiens 34,365 23-Nov-99 Contains CA repeat, STSs, GSSs and a CpG Island, complete sequence. GB_PL2:ATF21P8 85785 AL022347 Arabidopsis thaliana DNA chromosome 4, BAC clone F21P8 (ESSA project) Arabidopsis thaliana 34,325 9-Jun-99 GB_PL2:U89959 106973 U89959 Arabidopsis thaliana BAC T7I23, complete sequence. Arabidopsis thaliana 33,874 26-Jun-98 rxa02136 645 GB_PL2:ATAC005819 57752 AC005819 Arabidopsis thaliana chromosome II BAC T3A4 genomic sequence, complete Arabidopsis thaliana 34,123 3-Nov-98 sequence. GB_PL2:F15K9 71097 AC005278 Arabidopsis thaliana chromosome 1 BAC F15K9 sequence, complete Arabidopsis thaliana 31,260 7-Nov-98 sequence. GB_PL2:U89959 106973 U89959 Arabidopsis thaliana BAC T7I23, complete sequence. Arabidopsis thaliana 34,281 26-Jun-98 rxa02139 1962 GB_BA1:MTCY190 34150 Z70283 Mycobacterium tuberculosis H37Rv complete genome; segment 98/162. Mycobacterium tuberculosis 62,904 17-Jun-98 GB_BA1:MSGB1554CS 36548 L78814 Mycobacterium leprae cosmid B1554 DNA sequence. Mycobacterium leprae 36,648 15-Jun-96 GB_BA1:MSGB1551CS 36548 L78813 Mycobacterium leprae cosmid B1551 DNA sequence. Mycobacterium leprae 36,648 15-Jun-96 rxa02153 903 GB_BA2:AF049897 9196 AF049897 Corynebacterium glutamicum N-acetylglutamylphosphate reductase (argC), Corynebacterium glutamicum 99,104 1-Jul-98 ornithine acetyltransferase (argJ), N-acetylglutamate kinase (argB), acetylornithine transaminase (argD), ornithine carbamoyltransferase (argF), arginine repressor (argR), argininosuccinate synthase (argG), and argininosuccinate lyase (argH) genes, complete cds. GB_BA1:AF005242 1044 AF005242 Corynebacterium glutamicum N-acetylglutamate-5-semialdehyde Corynebacterium glutamicum 99,224 2-Jul-97 dehydrogenase (argC) gene, complete cds. GB_BA1:CGARGCJBD 4355 X86157 C glutamicum argC, argJ, argB, argD, and argF genes. Corynebacterium glutamicum 100,000 25-Jul-96 rxa02154 414 GB_BA2:AF049897 9196 AF049897 Corynebacterium glutamicum N-acetylglutamylphosphate reductase (argC), Corynebacterium glutamicum 98,551 1-Jul-98 ornithine acetyltransferase (argJ), N-acetylglutamate kinase (argB), acetylornithine transaminase (argD), ornithine carbamoyltransferase (argF), arginine repressor (argR), argininosuccinate synthase (argG), and argininosuccinate lyase (argH) genes, complete cds GB_BA1:AF005242 1044 AF005242 Corynebacterium glutamicum N-acetylglutamate-5-semialdehyde Corynebacterium glutamicum 98,477 2-Jul-97 dehydrogenase (argC) gene, complete cds. GB_BA1:CGARGCJBD 4355 X86157 C. glutamicum argC, argJ, argB, argD, and argF genes. Corynebacterium glutamicum 100,000 25-Jul-96 rxa02155 1287 GB_BA1:CGARGCJBD 4355 X86157 C. glutamicum argC, argJ, argB, argD, and argF genes. Corynebacterium glutamicum 99,767 25-Jul-96 GB_BA2:AF049897 9196 AF049897 Corynebacterium glutamicum N-acetylglutamylphosphate reductase (argC), Corynebacterium glutamicum 99,378 1-Jul-98 ornithine acetyltransferase (argJ), N-acetylglutamate kinase (argB), acetylornithine transaminase (argD), ornithine carbamoyltransferase (argF), arginine repressor (argR), argininosuccinate synthase (argG), and argininosuccinate lyase (argH) genes, complete cds. GB_BA1:MSGB1133CS 42106 L78811 Mycobacterium leprae cosmid B1133 DNA sequence. Mycobacterium leprae 55,504 15-Jun-96 rxa02156 1074 GB_BA2:AF049897 9196 AF049897 Corynebacterium glutamicum N-acetylglutamylphosphate reductase (argC), Corynebacterium glutamicum 100,000 1-Jul-98 ornithine acetyltransferase (argJ), N-acetylglutamate kinase (argB), acetylornithine transaminase (argD), ornithine carbamoyltransferase (argF), arginine repressor (argR), argininosuccinate synthase (argG), and argininosuccinate lyase (argH) genes, complete cds. GB_BA1:CGARGCJBD 4355 X86157 C. glutamicum argC, argJ, argB, argD, and argF genes. Corynebacterium glutamicum 100,000 25-Jul-96 GB_BA2:AE001816 10007 AE001816 Thermotoga maritima section 128 of 136 of the complete genome. Thermotoga maritima 50,238 2-Jun-99 rxa02157 1296 GB_BA2:AF049897 9196 AF049897 Corynebacterium glutamicum N-acetylglutamylphosphate reductase (argC), Corynebacterium glutamicum 99,612 1-Jul-98 ornithine acetyltransferase (argJ), N-acetylglutamate kinase (argB), acetylornithine transaminase (argD), ornithine carbamoyltransferase (argF), arginine repressor (argR), argininosuccinate synthase (argG), and argininosuccinate lyase (argH) genes, complete cds. GB_BA1:CGARGCJBD 4355 X86157 C. glutamicum argC, argJ, argB, argD, and argF genes. Corynebacterium glutamicum 99,612 25-Jul-96 GB_BA1:MTCY06H11 38000 Z85982 Mycobacterium tuberculosis H37Rv complete genome; segment 73/162. Mycobacterium tuberculosis 57,278 17-Jun-98 rxa02158 1080 GB_BA2:AF049897 9196 AF049897 Corynebacterium glutamicum N-acetylglutamylphosphate reductase (argC), Corynebacterium glutamicum 100,000 1-Jul-98 ornithine acetyltransferase (argJ), N-acetylglutamate kinase (argB), acetylornithine transaminase (argD), ornithine carbamoyltransferase (argF), arginine repressor (argR), argininosuccinate synthase (argG), and argininosuccinate lyase (argH) genes, complete cds. GB_BA2:AF031518 2045 AF031518 Corynebacterium glutamicum ornithine carbamolytransferase (argF) gene, Corynebacterium glutamicum 99,898 5-Jan-99 complete cds. GB_BA1:CGARGCJBD 4355 X86157 C. glutamicum argC, argJ, argB, argD, and argF genes. Corynebacterium glutamicum 100,000 25-Jul-96 rxa02159 636 GB_BA2:AF049897 9196 AF049897 Corynebacterium glutamicum N-acetylglutamylphosphate reductase (argC), Corynebacterium glutamicum 99,843 1-Jul-98 ornithine acetyltransferase (argJ), N-acetylglutamate kinase (argB), acetylornithine transaminase (argD), ornithine carbamoyltransferase (argF), arginine repressor (argR), argininosuccinate synthase (argG), and argininosuccinate lyase (argH) genes, complete cds. GB_BA2:AF031518 2045 AF031518 Corynebacterium glutamicum ornithine carbamolytransferase (argF) gene, Corynebacterium glutamicum 88,679 5-Jan-99 complete cds. GB_BA2:AF041436 516 AF041436 Corynebacterium glutamicum arginine repressor (argR) gene, complete cds. Corynebacterium glutamicum 100,000 5-Jan-99 rxa02160 1326 GB_BA2:AF049897 9196 AF049897 Corynebacterium glutamicum N-acetylglutamylphosphate reductase (argC), Corynebacterium glutamicum 99,774 1-Jul-98 ornithine acetyltransferase (argJ), N-acetylglutamate kinase (argB), acetylornithine transaminase (argD), ornithine carbamoyltransferase (argF), arginine repressor (argR), argininosuccinate synthase (argG), and argininosuccinate lyase (argH) genes, complete cds. GB_BA2:AF030520 1206 AF030520 Corynebacterium glutamicum argininosuccinate synthetase (argG) gene, Corynebacterium glutamicum 99,834 19-Nov-97 complete cds. GB_BA1:SCARGGH 1909 Z49111 S. clavuligerus argG gene and argH gene (partial). Streptomyces clavuligerus 65,913 22-Apr-96 rxa02162 1554 GB_BA2:AF049897 9196 AF049897 Corynebacterium glutamicum N-acetylglutamylphosphate reductase (argC), Corynebacterium glutamicum 88,524 1-Jul-98 ornithine acetyltransferase (argJ), N-acetylglutamate kinase (argB), acetylornithine transaminase (argD), ornithine carbamoyltransferase (argF), arginine repressor (argR), argininosuccinate synthase (argG), and argininosuccinate lyase (argH) genes, complete cds. GB_BA2:AF048764 1437 AF048764 Corynebacterium glutamicum argininosuccinate lyase (argH) gene, complete Corynebacterium glutamicum 87,561 1-Jul-98 cds. GB_BA1:MTCY06H11 38000 Z85982 Mycobacterium tuberculosis H37Rv complete genome; segment 73/162. Mycobacterium tuberculosis 64,732 17-Jun-98 rxa02176 1251 GB_BA1:MTCY31 37630 Z73101 Mycobacterium tuberculosis H37Rv complete genome; segment 41/162. Mycobacterium tuberculosis 36,998 17-Jun-98 GB_BA1:CGGLTG 3013 X66112 C. glutamicum glt gene for citrate synthase and ORF. Corynebacterium glutamicum 39,910 17-Feb-95 GB_PL2:PGU65399 2700 U65399 Basidiomycete CECT 20197 phenoloxidase (pox1) gene, complete cds. basidiomycete CECT 20197 38,474 19-Jul-97 rxa02189 861 GB_PR3:AC002468 115888 AC002468 Human Chromosome 15q26.1 PAC clone pDJ417d7, complete sequence. Homo sapiens 35,941 16-Sep-98 GB_BA1:MSGB1970CS 39399 L78815 Mycobacterium leprae cosmid B1970 DNA sequence. Mycobacterium leprae 40,286 15-Jun-96 GB_PR3:AC002468 115888 AC002468 Human Chromosome 15q26.1 PAC clone pDJ417d7, complete sequence. Homo sapiens 33,689 16-Sep-98 rxa02193 1701 GB_BA1:BRLASPA 1987 D25316 Brevibacterium flavum aspA gene for aspartase, complete cds. Corynebacterium glutamicum 99,353 6-Feb-99 GB_PAT:E04307 1581 E04307 DNA encoding Brevibacterium flavum aspartase. Corynebacterium glutamicum 99,367 29-Sep-97 GB_BA1:ECOUW93 338534 U14003 Escherichia coil K-12 chromosomal region from 92.8 to 00.1 minutes. Escherichia coli 37,651 17-Apr-96 rxa02194 966 GB_BA2:AF050166 840 AF050166 Corynebacterium glutamicum ATP phosphoribosyltransferase (hisG) gene, Corynebacterium glutamicum 98,214 5-Jan-99 complete cds. GB_BA1:BRLASPA 1987 D25316 Brevibacterium flavum aspA gene for aspartase, complete cds. Corynebacterium glutamicum 93,805 6-Feb-99 GB_PAT:E08649 188 E08649 DNA encoding part of aspartase from coryneform bacteria. Corynebacterium glutamicum 100,000 29-Sep-97 rxa02195 393 GB_BA2:AF086704 264 AF086704 Corynebacterium glutamicum phosphoribosyl-ATP-pyrophosphohydrolase Corynebacterium glutamicum 100,000 8-Feb-99 (hisE) gene, complete cds GB_BA1:EAY17145 6019 Y17145 Eubacterium acidaminophilum grdR, grdl, grdH genes and partial ldc, grdT Eubacterium 39,075 5-Aug-98 genes. acidaminophilum GB_STS:G01195 332 G01195 fruit fly STS Dm1930 clone DS06959 T7. Drosophila melanogaster 35,542 28-Feb-95 rxa02197 551 GB_BA1:MTCY261 27322 Z97559 Mycobacterium tuberculosis H37Rv complete genome; segment 95/162. Mycobacterium tuberculosis 33,938 17-Jun-98 GB_BA1:MLCB2533 40245 AL035310 Mycobacterium leprae cosmid B2533. Mycobacterium leprae 65,517 27-Aug-99 GB_BA1:U00017 42157 U00017 Mycobacterium leprae cosmid B2126. Mycobacterium leprae 36,770 01-MAR-1994 rxa02198 2599 GB_BA1:U00017 42157 U00017 Mycobacterium leprae cosmid B2126 Mycobacterium leprae 38,674 01-MAR-1994 GB_BA1:MLCB2533 40245 AL035310 Mycobacterium leprae cosmid B2533. Mycobacterium leprae 65,465 27-Aug-99 GB_BA1:MTCY261 27322 Z97559 Mycobacterium tuberculosis H37Rv complete genome; segment 95/162. Mycobacterium tuberculosis 37,577 17-Jun-98 rxa02208 1025 GB_BA1:U00017 42157 U00017 Mycobacterium leprae cosmid B2126. Mycobacterium leprae 59,823 01-MAR-1994 GB_BA1:AP000063 185300 AP000063 Aeropyrum pernix genomic DNA, section 6/7. Aeropyrum pernix 39,442 22-Jun-99 GB_PR4:AC006236 127593 AC006236 Homo sapiens chromosome 17, clone hCIT.162_E_12, complete sequence. Homo sapiens 37,191 29-DEC-1998 rxa02229 948 GB_BA1:MSGY154 40221 AD000002 Mycobacterium tuberculosis sequence from clone y154. Mycobacterium tuberculosis 53,541 03-DEC-1996 GB_BA1:MTCY154 13935 Z98209 Mycobacterium tuberculosis H37Rv complete genome; segment 121/162. Mycobacterium tuberculosis 40,407 17-Jun-98 GB_BA1:U00019 36033 U00019 Mycobacterium leprae cosmid B2235, Mycobacterium leprae 40,541 01-MAR-1994 rxa02234 3462 GB_BA1:MSGB937CS 38914 L78820 Mycobacterium leprae cosmid B937 DNA sequence. Mycobacterium leprae 66,027 15-Jun-96 GB_BA1:MTCY2B12 20431 Z81011 Mycobacterium tuberculosis H37Rv complete genome; segment 61/162. Mycobacterium tuberculosis 71,723 18-Jun-98 GB_BA2:U01072 4393 U01072 Mycobacterium bovis BCG orotidine-5′-monophosphate decarboxylase (uraA) Mycobacterium bovis 67,101 22-DEC-1993 gene. rxa02235 727 GB_BA1:MSU91572 960 U91572 Mycobacterium smegmatis carbamoyl phosphate synthetase (pyrAB) gene, Mycobacterium smegmatis 60,870 22-MAR-1997 partial cds and orotidine 5′-monophosphate decarboxylase (pyrF) gene. complete cds. GB_HTG3:AC009364 192791 AC009364 Homo sapiens chromosome 7, *** SEQUENCING IN PROGRESS ***, 57 Homo sapiens 37,994 1-Sep-99 unordered pieces. GB_HTG3:AC009364 192791 AC009364 Homo sapiens chromosome 7, *** SEQUENCING IN PROGRESS ***, 57 Homo sapiens 37,994 1-Sep-99 unordered pieces. rxa02237 693 GB_BA1:MTCY21B4 39150 Z80108 Mycobacterium tuberculosis H37Rv complete genome; segment 62/162. Mycobacterium tuberculosis 55,844 23-Jun-98 GB_BA2:AF077324 5228 AF077324 Rhodococcus equi strain 103 plasmid RE-VP1 fragment f. Rhodococcus equi 41,185 5-Nov-98 GB_EST22:AU017763 586 AU017763 AU017763 Mouse two-cell stage embryo cDNA Mus musculus cDNA clone Mus musculus 38,616 19-OCT-1998 J0744A04 3′, mRNA sequence. rxa02239 1389 GB_BA1:MTCY21B4 39150 Z80108 Mycobacterium tuberculosis H37Rv complete genome; segment 62/162. Mycobacterium tuberculosis 56,282 23-Jun-98 GB_HTG3:AC010745 193862 AC010745 Homo sapiens clone NH0549D18, *** SEQUENCING IN PROGRESS ***, 30 Homo sapiens 36,772 21-Sep-99 unordered pieces. GB_HTG3:AC010745 193862 AC010745 Homo sapiens clone NH0549D18, *** SEQUENCING IN PROGRESS ***, 30 Homo sapiens 36,772 21-Sep-99 unordered pieces. rxa02240 1344 EM_PAT:E09855 1239 E09855 gDNA encoding S-adenosylmethionine synthetase. Corynebacterium glutamicum 99,515 07-OCT-1997 (Rel. 52, Created) GB_PAT:A37831 5392 A37831 Sequence 1 from Patent WO9408014. Streptomyces pristinaespiralis 63,568 05-MAR-1997 GB_BA2:AF117274 2303 AF117274 Streptomyces spectabilis flavoprotein homolog Dfp (dfp) gene, partial cds, and Streptomyces spectabilis 65,000 31-MAR-1999 S-adenosylmethionine synthetase (metK) gene, complete cds. rxa02246 1107 EM_BA1:AB003693 5589 AB003693 Corynebacterium ammoniagenes DNA for rib operon, complete cds. Corynebacterium 52,909 03-OCT-1997 ammoniagenes (Rel. 52, Created) GB_PAT:E07957 5589 E07957 gDNA encoding at least guanosine triphosphate cyclohydrolase and riboflavin Corynebacterium 52,909 29-Sep-97 synthase. ammoniagenes GB_PAT:I32742 5589 I32742 Sequence 1 from U.S. Pat. 5589355. Unknown. 52,909 6-Feb-97 rxa02247 756 GB_PAT:I32743 2689 I32743 Sequence 2 from U.S. Pat. 5589355. Unknown. 57,937 6-Feb-97 EM_BA1:AB003693 5589 AB003693 Corynebacterium ammoniagenes DNA for rib operon, complete cds. Corynebacterium 57,937 03-OCT-1997 ammoniagenes (Rel. 52, Created) GB_PAT:I32742 5589 I32742 Sequence 1 from U.S. Pat. 5589355. Unknown. 57,937 6-Feb-97 rxa02248 1389 GB_PAT:I32742 5589 I32742 Sequence 1 from U.S. Pat. 5589355 Unknown. 61,843 6-Feb-97 EM_BA1:AB003693 5589 AB003693 Corynebacterium ammoniagenes DNA for rib operon, complete cds. Corynebacterium 61,843 03-OCT-1997 ammoniagenes (Rel. 52, Created) GB_PAT:E07957 5589 E07957 gDNA encoding at least guanosine triphosphate cyclohydrolase and riboflavin Corynebacterium 61,843 29-Sep-97 synthase. ammoniagenes rxa02249 600 GB_PAT:E07957 5589 E07957 gDNA encoding at least guanosine triphosphate cyclohydrolase and riboflavin Corynebacterium 64,346 29-Sep-97 synthase. ammoniagenes GB_PAT:I32742 5589 I32742 Sequence 1 from U.S. Pat. 5589355. Unknown. 64,346 6-Feb-97 GB_PAT:I32743 2689 I32743 Sequence 2 from U.S. Pat. 5589355. Unknown. 64,346 6-Feb-97 rxa02250 643 GB_PAT:E07957 5589 E07957 gDNA encoding at least guanosine triphosphate cyclohydrolase and riboflavin Corynebacterium 56,318 29-Sep-97 synthase. ammoniagenes GB_PAT:I32742 5589 I32742 Sequence 1 from U.S. Pat. 5589355. Unknown. 56,318 6-Feb-97 EM_BA1:AB003693 5589 AB003693 Corynebacterium ammoniagenes DNA for rib operon, complete cds. Corynebacterium 56,318 03-OCT-1997 ammoniagenes (Rel. 52, Created) rxa02262 1269 GB_BA1:CGL007732 4460 AJ007732 Corynebacterium glutamicum 3′ ppc gene, secG gene, amt gene, ocd gene Corynebacterium glutamicum 100,000 7-Jan-99 and 5′ soxA gene GB_BA1:CGAMTGENE 2028 X93513 C. glutamicum amt gene. Corynebacterium glutamicum 100,000 29-MAY-1996 GB_VI:HEHCMVCG 229354 X17403 Human cytomegalovirus strain AD169 complete genome. human herpesvirus 5 38,651 10-Feb-99 rxa02263 488 GB_BA1:CGL007732 4460 AJ007732 Corynebacterium glutamicum 3′ ppc gene, secG gene, amt gene, ocd gene Corynebacterium glutamicum 100,000 7-Jan-99 and 5′ soxA gene. GB_BA1:CGL007732 4460 AJ007732 Corynebacterium glutamicum 3′ ppc gene, secG gene, amt gene, ocd gene Corynebacterium glutamicum 37,526 7-Jan-99 and 5′ soxA gene. rxa02272 1368 EM_PAT:E09373 1591 E09373 Creatinine deiminase gene. Bacillus sp. 96,928 08-OCT-1997 (Rel. 52, Created) GB_BA1:D38505 1591 D38505 Bacillus sp. gene for creatinine deaminase, complete cds. Bacillus sp. 96,781 7-Aug-98 GB_HTG2:AC006595 146070 AC006595 Homo sapiens , *** SEQUENCING IN PROGRESS ***, 4 unordered pieces. Homo sapiens 36,264 20-Feb-99 rxa02281 1545 GB_GSS12:AQ411010 551 AQ411010 HS_2257_B1_H02_MR CIT Approved Human Genomic Sperm Library D Homo sapiens 36,197 17-MAR-1999 Homo sapiens genomic clone Plate = 2257 Col = 3 Row = P, genomic survey sequence. GB_EST23:AI128623 363 AI128623 qa62c01.s1 Soares_fetal_heart_NbHH19W Homo sapiens cDNA clone Homo sapiens 37,017 05-OCT-1998 IMAGE:1691328 3′, mRNA sequence. GB_PL2.ATAC007019 102335 AC007019 Arabidopsis thaliana chromosome II BAC F7D8 genomic sequence, complete Arabidopsis thaliana 33,988 16-MAR-1999 sequence. rxa02299 531 GB_BA2:AF116184 540 AF116184 Corynebacterium glutamicum L-aspartate-alpha-decarboxylase precursor Corynebacterium glutamicum 100,000 02-MAY-1999 (panD) gene, complete cds. GB_GSS9:AQ164310 507 AQ164310 HS_2171_A2_E01_MR CIT Approved Human Genomic Sperm Library D Homo sapiens 37,278 16-OCT-1998 Homo sapiens genomic clone Plate = 2171 Col = 2 Row = I, genomic survey sequence. GB_VI:MH68TKH 4557 X93468 Murine herpesvirus type 68 thymidine kinase and glycoprotein H genes. murine herpesvirus 68 40,288 3-Sep-96 rxa02311 813 GB_HTG4:AC006091 176878 AC006091 Drosophila melanogaster chromosome 3 clone BACR48G05 (D475) RPCI-98 Drosophila melanogaster 36,454 27-OCT-1999 48.G.5 map 91F1-91F13 strain y; cn bw sp, *** SEQUENCING IN PROGRESS ***, 4 unordered pieces GB_HTG4:AC006091 176878 AC006091 Drosophila melanogaster chromosome 3 clone BACR48G05 (D475) RPCI-98 Drosophila melanogaster 36,454 27-OCT-1999 48.G.5 map 91F1-91F13 strain y; cn bw sp, *** SEQUENCING IN PROGRESS ***, 4 unordered pieces. GB_BA2:RRU65510 16259 U65510 Rhodospirillum rubrum CO-induced hydrogenase operon (cooM, cooK, cooL, Rhodospirillum rubrum 37,828 9-Apr-97 cooX, cooU, cooH) genes, iron sulfur protein (cooF) gene, carbon monoxide dehydrogenase (cooS) gene, carbon monoxide dehydrogenase accessory proteins (cooC, cooT, cooJ) genes, putative transcriptional activator (cooA) gene, nicotinate-nucleotide pyrophosphorylase (nadC) gene, complete cds, L-aspartate oxidase (nadB) gene, and alkyl hydropperoxide reductase (ahpC) gene, partial cds. rxa02315 1752 GB_BA1:MSGY224 40051 AD000004 Mycobacterium tuberculosis sequence from clone y224. Mycobacterium tuberculosis 49,418 03-DEC-1996 GB_BA1:MTY25D10 40838 Z95558 Mycobacterium tuberculosis H37Rv complete genome; segment 28/162. Mycobacterium tuberculosis 49,360 17-Jun-98 GB_BA1:MSGY224 40051 AD000004 Mycobacterium tuberculosis sequence from clone y224. Mycobacterium tuberculosis 38,150 03-DEC-1996 rxa02318 402 GB_HTG3:AC011348 111083 AC011348 Homo sapiens chromosome 5 clone CIT-HSPC_303E13, *** SEQUENCING Homo sapiens 35,821 06-OCT-1999 IN PROGRESS ***, 3 ordered pieces. GB_HTG3:AC011348 111083 AC011348 Homo sapiens chromosome 5 clone CIT-HSPC_303E13, *** SEQUENCING Homo sapiens 35,821 06-OCT-1999 IN PROGRESS ***, 3 ordered pieces. GB_HTG3:AC011412 89234 AC011412 Homo sapiens chromosome 5 clone CIT978SKB_81K21, *** SEQUENCING Homo sapiens 36,181 06-OCT-1999 IN PROGRESS ***, 3 ordered pieces. rxa02319 1080 GB_BA1:MSGY224 40051 AD000004 Mycobacterium tuberculosis sequence from clone y224. Mycobacterium tuberculosis 37,792 03-DEC-1996 GB_BA1:MTY25D10 40838 Z95558 Mycobacterium tuberculosis H37Rv complete genome; segment 28/162. Mycobacterium tuberculosis 37,792 17-Jun-98 GB_EST23:AI117213 476 AI117213 ub83h02.r1 Soares 2NbMT Mus musculus cDNA clone IMAGE:1395123 Mus musculus 35,084 2-Sep-98 5′, mRNA sequence. rxa02345 1320 GB_BA1:BAPURKE 2582 X91189 B. ammoniagenes purK and purE genes. Corynebacterium 61,731 14-Jan-97 ammoniagenes GB_BA1:MTCY71 42729 Z92771 Mycobacterium tuberculosis H37Rv complete genome; segment 141/162. Mycobacterium tuberculosis 39,624 10-Feb-99 GB_BA1:MTCY71 42729 Z92771 Mycobacterium tuberculosis H37Rv complete genome; segment 141/162. Mycobacterium tuberculosis 39,847 10-Feb-99 rxa02350 618 GB_BA1:BAPURKE 2582 X91189 B. ammoniagenes purK and purE genes. Corynebacterium 64,286 14-Jan-97 ammoniagenes GB_PL1:SC130KBXV 129528 X94335 S. cerevisiae 130kb DNA fragment from chromosome XV. Saccharomyces cerevisiae 36,617 15-Jul-97 GB_PL1:SCXVORFS 50984 X90518 S. cerevisiae DNA of 51 Kb from chromosome XV right arm. Saccharomyces cerevisiae 36,617 1-Nov-95 rxa02373 1038 GB_PAT:E00311 1853 E00311 DNA coding of 2,5-diketogluconic acid reductase. unidentified 56,123 29-Sep-97 GB_PAT:I06030 1853 I06030 Sequence 4 from Patent EP 0305608. Unknown. 56,220 02-DEC-1994 GB_PAT:I00836 1853 I00836 Sequence 1 from U.S. Pat. 4758514. Unknown. 56,220 21-MAY-1993 rxa02375 1350 GB_BA2:CGU31230 3005 U31230 Corynebacterium glutamicum Obg protein homolog gene, partial cds, gamma Corynebacterium glutamicum 99,332 2-Aug-96 glutamyl kinase (proB) gene, complete cds, and (unkdh) gene, complete cds. GB_HTG3:AC009946 169072 AC009946 Homo sapiens clone NH0012C17, *** SEQUENCING IN PROGRESS ***, 1 Homo sapiens 36,115 8-Sep-99 unordered pieces. GB_HTG3:AC009946 169072 AC009946 Homo sapiens clone NH0012C17, *** SEQUENCING IN PROGRESS ***, 1 Homo sapiens 36,115 8-Sep-99 unordered pieces. rxa02380 777 GB_BA1:MTCY253 41230 Z81368 Mycobacterium tuberculosis H37Rv complete genome; segment 106/162. Mycobacterium tuberculosis 38,088 17-Jun-98 GB_HTG4:AC010658 120754 AC010658 Drosophila melanogaster chromosome 3L/75C1 clone RPCI98-3B20, *** Drosophila melanogaster 35,817 16-OCT-1999 SEQUENCING IN PROGRESS ***, 78 unordered pieces. GB_HTG4:AC010658 120754 AC010658 Drosophila melanogaster chromosome 3L/75C1 clone RPCI98-3B20, *** Drosophila melanogaster 35,817 16-OCT-1999 SEQUENCING IN PROGRESS ***, 78 unordered pieces.7 rxa02382 1419 GB_BA1:CGPROAGEN 1783 X82929 C. glutamicum proA gene. Corynebacterium glutamicum 98,802 23-Jan-97 GB_BA1:MTCY428 26914 Z81451 Mycobacterium tuberculosis H37Rv complete genome; segment 107/162. Mycobacterium tuberculosis 38,054 17-Jun-98 GB_BA2:CGU31230 3005 U31230 Corynebacterium glutamicum Obg protein homolog gene, partial cds, gamma Corynebacterium glutamicum 98,529 2-Aug-96 glutamyl kinase (proB) gene, complete cds, and (unkdh) gene, complete cds. rxa02400 693 GB_BA1:CGACEA 2427 X75504 C. glutamicum aceA gene and thiX genes (partial). Corynebacterium glutamicum 100,000 9-Sep-94 GB_PAT:I86191 2135 I86191 Sequence 3 from U.S. Pat. 5700661. Unknown. 100,000 10-Jun-98 GB_PAT:I13693 2135 I13693 Sequence 3 from U.S. Pat. 5439822. Unknown. 100,000 26-Sep-95 rxa02432 1098 GB_GSS15:AQ606842 574 AQ606842 HS_5404_B2_E07_T7A RPCI-11 Human Male BAC Library Homo sapiens Homo sapiens 39,716 10-Jun-99 genomic clone Plate = 980 Col = 14 Row = J, genomic survey sequence. GB_EST1:T05804 406 T05804 EST03693 Fetal brain, Stratagene (cat#936206) Homo sapiens cDNA clone Homo sapiens 37,915 30-Jun-93 HFBDG63 similar to EST containing Alu repeat, mRNA sequence. GB_PL1:AB006699 77363 AB006699 Arabidopsis thaliana genomic DNA, chromosome 5, P1 clone: MDJ22, Arabidopsis thaliana 35,526 20-Nov-99 complete sequence. rxa02458 1413 GB_BA2:AF114233 1852 AF114233 Corynebacterium glutamicum 5-enolpyruvylshikimate 3-phosphate synthase Corynebacterium glutamicum 100,000 7-Feb-99 (aroA) gene, complete cds GB_EST37:AW013061 578 AW013061 ODT-0033 Winter flounder ovary Pleuronectes americanus cDNA clone ODT- Pleuronectes americanus 39,175 10-Sep-99 0033 5′ similar to FRUCTOSE-BISPHOSPHATE ALDOLASE B (LIVER), mRNA sequence. GB_GSS15:AQ650027 728 AQ650027 Sheared DNA-5L2.TF Sheared DNA Trypanosoma brucei genomic clone Trypanosoma brucei 39,281 22-Jun-99 Sheared DNA-5L2, genomic survey sequence. rxa02469 1554 GB_BA1:MTCY359 36021 Z83859 Mycobacterium tuberculosis H37Rv complete genome; segment 84/162. Mycobacterium tuberculosis 39,634 17-Jun-98 GB_BA1:MLCB1788 39228 AL008609 Mycobacterium leprae cosmid B1788. Mycobacterium leprae 59,343 27-Aug-99 GB_BA1:SCAJ10601 4692 AJ010601 Streptomyces coelicolor A3 (2) DNA for whiD and whiK loci. Streptomyces coelicolor 48,899 17-Sep-98 rxa02497 1050 GB_BA2:CGU31224 422 U31224 Corynebacterium glutamicum (ppx) gene, partial cds. Corynebacterium glutamicum 96,445 2-Aug-96 GB_BA1:MTCY20G9 37218 Z77162 Mycobacterium tuberculosis H37Rv complete genome; segment 25/162. Mycobacterium tuberculosis 59,429 17-Jun-98 GB_BA1:SCE7 16911 AL049819 Streptomyces coelicolor cosmid E7. Streptomyces coelicolor 39,510 10-MAY-1999 rxa02499 933 GB_BA2:CGU31225 1817 U31225 Corynebacterium glutamicum L-proline:NADP + 5-oxidoreductase (proC) gene, Corynebacterium glutamicum 97,749 2-Aug-96 complete cds. GB_BA1:NG17PILA 1920 X13965 Neisseria gonorrhoeae pilA gene. Neisseria gonorrhoeae 43,249 30-Sep-93 GB_HTG2:AC007984 129715 AC007984 Drosophila melanogaster chromosome 3 clone BACR05C10 (D781) RPCI-98 Drosophila melanogaster 33,406 2-Aug-99 05.C.10 map 97D-97E strain y; cn bw sp, *** SEQUENCING IN PROGRESS ***, 87 unordered pieces. rxa02501 1188 GB_BA1:MTCY20G9 37218 Z77162 Mycobacterium tuberculosis H37Rv complete genome; segment 25/162. Mycobacterium tuberculosis 39,357 17-Jun-98 GB_BA1:U00018 42991 U00018 Mycobacterium leprae cosmid B2168. Mycobacterium leprae 51,768 01-MAR-1994 GB_VI:HE1CG 152261 X14112 Herpes simplex virus (HSV) type 1 complete genome. human herpesvirus 1 39,378 17-Apr-97 rxa02503 522 GB_PR3:AC005328 35414 AC005328 Homo sapiens chromosome 19, cosmid R26660, complete sequence. Homo sapiens 39,922 28-Jul-98 GB_PR3:AC005545 43514 AC005545 Homo sapiens chromosome 19, cosmid R26634, complete sequence. Homo sapiens 39,922 3-Sep-98 GB_PR3:AC005328 35414 AC005328 Homo sapiens chromosome 19, cosmid R26660, complete sequence. Homo sapiens 34,911 28-Jul-98 rxa02504 681 GB_BA1:MTCY20G9 37218 Z77162 Mycobacterium tuberculosis H37Rv complete genome; segment 25/162. Mycobacterium tuberculosis 54,940 17-Jun-98 GB_PR3:AC005328 35414 AC005328 Homo sapiens chromosome 19, cosmid R26660, complete sequence. Homo sapiens 41,265 28-Jul-98 GB_PR3:AC005545 43514 AC005545 Homo sapiens chromosome 19, cosmid R26634, complete sequence Homo sapiens 41,265 3-Sep-98 rxa02516 1386 GB_BA1:MLCL536 36224 Z99125 Mycobacterium leprae cosmid L536. Mycobacterium leprae 37,723 04-DEC-1998 GB_BA1:U00013 35881 U00013 Mycobacterium leprae cosmid B1496. Mycobacterium leprae 37,723 01-MAR-1994 GB_BA1:MTV007 32806 AL021184 Mycobacterium tuberculosis H37Rv complete genome; segment 64/162. Mycobacterium tuberculosis 61,335 17-Jun-98 rxa02517 570 GB_BA1:MLCL536 36224 Z99125 Mycobacterium leprae cosmid L536. Mycobacterium leprae 37,018 04-DEC-1998 GB_BA1:U00013 35881 U00013 Mycobacterium leprae cosmid B1496. Mycobacterium leprae 37,018 01-MAR-1994 GB_BA1:SCC22 22115 AL096839 Streptomyces coelicolor cosmid C22. Streptomyces coelicolor 37,071 12-Jul-99 rxa02532 1170 GB_OV:AF137219 831 AF137219 Amia calva mixed lineage leukemia-like protein (MII) gene, partial cds. Amia calva 36,853 7-Sep-99 GB_EST30:AI645057 301 AI645057 vs52a10.y1 Stratagene mouse Tcell 937311 Mus musculus cDNA clone Mus musculus 41,860 29-Apr-99 IMAGE:1149882 5′, mRNA sequence GB_EST20:AA822595 429 AA822595 vs52a10.r1 Stratagene mouse Tcell 937311 Mus musculus cDNA clone Mus musculus 42,353 17-Feb-98 IMAGE:1149882 5′, mRNA sequence. rxa02536 879 GB_HTG2:AF130866 118874 AF130866 Homo sapiens chromosome 8 clone PAC 172N13 map 8q24, *** Homo sapiens 40,754 21-MAR-1999 SEQUENCING IN PROGRESS ***, in unordered pieces. GB_HTG2:AF130866 118874 AF130866 Homo sapiens chromosome 8 clone PAC 172N13 map 8q24, *** Homo sapiens 40,754 21-MAR-1999 SEQUENCING IN PROGRESS ***, in unordered pieces. GB_PL1:ATT12J5 84499 AL035522 Arabidopsis thaliana DNA chromosome 4, BAC clone T12J5 (ESSAII project). Arabidopsis thaliana 35,063 24-Feb-99 rxa02550 1434 GB_BA1:MTCY279 9150 Z97991 Mycobacterium tuberculosis H37Rv complete genome; segment 17/162. Mycobacterium tuberculosis 37,773 17-Jun-98 GB_BA1:MSGB1970CS 39399 L78815 Mycobacterium leprae cosmid B1970 DNA sequence. Mycobacterium leprae 39,024 15-Jun-96 GB_BA2:SC2H4 25970 AL031514 Streptomyces coelicolor cosmid 2H4. Streptomyces coelicolor 37,906 19-OCT-1999 A3 (2) rxa02559 1026 GB_BA1:MTV004 69350 AL009198 Mycobacterium tuberculosis H37Rv complete genome; segment 144/162. Mycobacterium tuberculosis 47,358 18-Jun-98 GB_PAT:I28684 5100 I28684 Sequence 1 from U.S. Pat. 5573915. Unknown. 39,138 6-Feb-97 GB_BA1:MTU27357 5100 U27357 Mycobacterium tuberculosis cyclopropane mycolic acid synthase (cma1) gene, Mycobacterium tuberculosis 39,138 26-Sep-95 complete cds. rxa02622 1683 GB_BA2:AE001780 11997 AE001780 Thermotoga maritima section 92 of 136 of the complete genome. Thermotoga maritima 44,914 2-Jun-99 GB_OV:AF064564 49254 AF064564 Fugu rubripes neurofibromatosis type 1 (NF1), A-kinase anchor protein Fugu rubripes 39,732 17-Aug-99 (AKAP84), BAW protein (BAW), and WSB1 protein (WSB1) genes, complete cds. GB_OV:AF064564 49254 AF064564 Fugu rubripes neurofibromatosis type 1 (NF1), A-kinase anchor protein Fugu rubripes 36,703 17-Aug-99 (AKAP84), BAW protein (BAW), and WSB1 protein (WSB1) genes, complete cds. rxa02623 714 GB_GSS5:AQ818728 444 AQ818728 HS_5268_A1_G09_SP6E RPCI-11 Human Male BAC Library Homo sapiens Homo sapiens 38,801 26-Aug-99 genomic clone Plate = 844 Col = 17 Row = M, genomic survey sequence. GB_HTG5:AC011083 198586 AC011083 Homo sapiens chromosome 9 clone RP11-111M7 map 9, WORKING DRAFT Homo sapiens 35,714 19-Nov-99 SEQUENCE, 51 unordered pieces. GB_GSS6:AQ826948 544 AQ826948 HS_5014_A2_C12_T7A RPCI-11 Human Male BAC Library Homo sapiens Homo sapiens 39,146 27-Aug-99 genomic clone Plate = 590 Col = 24 Row = E, genomic survey sequence. rxa02629 708 GB_VI:BRSMGP 462 M86652 Bovine respiratory syncytial virus membrane glycoprotein mRNA, complete Bovine respiratory syncytial 37,013 28-Apr-93 cds. virus GB_VI:BRSMGP 462 M86652 Bovine respiratory syncytial virus membrane glycoprotein mRNA, complete Bovine respiratory syncytial 37,013 28-Apr-93 cds. virus rxa02645 1953 GB_PAT:A45577 1925 A45577 Sequence 1 from Patent WO9519442. Corynebacterium glutamicum 39,130 07-MAR-1997 GB_PAT:A45581 1925 A45581 Sequence 5 from Patent WO9519442. Corynebacterium glutamicum 39,130 07-MAR-1997 GB_BA1:CORILVA 1925 L01508 Corynebacterium glutamicum threonine dehydratase (ilvA) gene, complete Corynebacterium glutamicum 39,130 26-Apr-93 cds. rxa02646 1392 GB_BA1:CORILVA 1925 L01508 Corynebacterium glutamicum threonine dehydratase (ilvA) gene, complete Corynebacterium glutamicum 99,138 26-Apr-93 cds. GB_PAT:A45585 1925 A45585 Sequence 9 from Patent WO9519442. Corynebacterium glutamicum 99,066 07-MAR-1997 GB_PAT:A45583 1925 A45583 Sequence 7 from Patent WO9519442. Corynebacterium glutamicum 99,066 07-MAR-1997 rxa02648 1326 GB_OV:ICTCNC 2049 M83111 Ictalurus punctatus cyclic nucleotide-gated channel RNA sequence. Ictalurus punctatus 38,402 24-MAY-1993 GB_EST11:AA265464 345 AA265464 mx91c06.r1 Soares mouse NML Mus musculus cDNA clone IMAGE:693706 Mus musculus 38,655 20-MAR-1997 5′, mRNA sequence. GB_GSS8:AQ006950 480 AQ006950 CIT-HSP-2294E14.TR CIT-HSP Homo sapiens genomic clone 2294E14, Homo sapiens 36,074 27-Jun-98 genomic survey sequence. rxa02653 rxa02687 1068 GB_BA1:CORPHEA 1088 M13774 C. glutamicum pheA gene encoding prephenate dehydratase, complete cds. Corynebacterium glutamicum 99,715 26-Apr-93 GB_PAT:E04483 948 E04483 DNA encoding prephenate dehydratase. Corynebacterium glutamicum 98,523 29-Sep-97 GB_PAT:E06110 948 E06110 DNA encoding prephenate dehydratase. Corynebacterium glutamicum 98,523 29-Sep-97 rxa02717 1005 GB_PL1:HVCH4H 59748 Y14573 Hordeum vulgare DNA for chromosome 4H. Hordeum vulgare 36,593 25-MAR-1999 GB_PR2:HS310H5 29718 Z69705 Human DNA sequence from cosmid 310H5 from a contig from the tip of the Homo sapiens 36,089 22-Nov-99 short arm of chromosome 16, spanning 2Mb of 16p13.3. Contains EST and CpG island. GB_PR3:AC004754 39188 AC004754 Homo sapiens chromosome 16, cosmid clone RT286 (LANL), complete Homo sapiens 36,089 28-MAY-1998 sequence. rxa02754 1461 GB_HTG2:AC008223 130212 AC008223 Drosophila melanogaster chromosome 3 clone BACR16I18 (D815) RPCI-98 Drosophila melanogaster 32,757 2-Aug-99 16.I.18 map 95A-95A strain y; cn bw sp, *** SEQUENCING IN PROGRESS ***, 101 unordered pieces. GB_HTG2:AC008223 130212 AC008223 Drosophila melanogaster chromosome 3 clone BACR16I18 (D815) RPCI-98 Drosophila melanogaster 32,757 2-Aug-99 16.I.18 map 95A-95A strain y; cn bw sp, *** SEQUENCING IN PROGRESS ***, 101 unordered pieces. GB_BA1:MTCY71 42729 Z92771 Mycobacterium tuberculosis H37Rv complete genome; segment 141/162. Mycobacterium tuberculosis 37,838 10-Feb-99 rxa02758 1422 GB_HTG5:AC011678 171967 AC011678 Homo sapiens clone 14_B_7, *** SEQUENCING IN PROGRESS ***, 20 Homo sapiens 35,331 5-Nov-99 unordered pieces. GB_HTG5:AC011678 171967 AC011678 Homo sapiens clone 14_B_7, *** SEQUENCING IN PROGRESS ***, 20 Homo sapiens 33,807 5-Nov-99 unordered pieces. GB_BA2:AF064070 23183 AF064070 Burkholderia pseudomallei putative dihydroorotase (pyrC) gene, partial cds; Burkholderia pseudomallei 36,929 20-Jan-99 putative 1-acyl-sn-glycerol-3-phosphate acyltransferase (plsC), putative diadenosine tetraphosphatase (apaH), complete cds; type II O-antigen biosynthesis gene cluster, complete sequence; putative undecaprenyl phosphate N-acetylglucosaminyltransferase, and putative UDP-glucose 4- epimerase genes, complete cds; and putative galactosyl transferase gene, partial cds. rxa02771 678 GB_BA2:AF038651 4077 AF038651 Corynebacterium glutamicum dipeptide-binding protein (dciAE) gene, partial Corynebacterium glutamicum 99,852 14-Sep-98 cds; adenine phosphoribosyltransferase (apt) and GTP pyrophosphokinase (rel) genes, complete cds; and unknown gene. GB_IN1:CELT19B4 37121 U80438 Caenorhabditis elegans cosmid T19B4. Caenorhabditis elegans 43,836 04-DEC-1996 GB_EST36:AV193572 360 AV193572 AV193572 Yuji Kohara unpublished cDNA:Strain N2 hermaphrodite embryo Caenorhabditis elegans 48,588 22-Jul-99 Caenorhabditis elegans cDNA clone yk618h8 5′, mRNA secquence. rxa02772 1158 GB_BA2:AF038651 4077 AF038651 Corynebacterium glutamicum dipeptide-binding protein (dciAE) gene, partial Corynebacterium glutamicum 99,914 14-Sep-98 cds; adenine phosphoribosyltransferase (apt) and GTP pyrophosphokinase (rel) genes, complete cds; and unknown gene. GB_BA1:MTCY227 35946 Z77724 Mycobacterium tuberculosis H37Rv complete genome; segment 114/162. Mycobacterium tuberculosis 38,339 17-Jun-98 GB_BA1:U00011 40429 U00011 Mycobacterium leprae cosmid B1177 Mycobacterium leprae 38,996 01-MAR-1994 rxa02790 1266 GB_BA1:MTCY159 33818 Z83863 Mycobacterium tuberculosis H37Rv complete genome; segment 111/162. Mycobacterium tuberculosis 37,640 17-Jun-98 GB_PR4:AC006581 172931 AC006581 Homo sapiens 12p21 BAC RPCI11-259O18 (Roswell Park Cancer Institute Homo sapiens 37,906 3-Jun-99 Human BAC Library) complete sequence. GB_PR4:AC006581 172931 AC006581 Homo sapiens 12p21 BAC RPCI11-259O18 (Roswell Park Cancer Institute Homo sapiens 35,280 3-Jun-99 Human BAC Library) complete sequence. rxa02791 951 GB_BA1:MTCY159 33818 Z83863 Mycobacterium tuberculosis H37Rv complete genome; segment 111/162. Mycobacterium tuberculosis 39,765 17-Jun-98 GB_OV:CHKCEK2 3694 M35195 Chicken tyrosine kinase (cek2) mRNA, complete cds. Gallus gallus 38,937 28-Apr-93 GB_BA1:MSASDASK 5037 Z17372 M. smegmatis asd, ask-alpha, and ask-beta genes. Mycobacterium smegmatis 38,495 9-Aug-94 rxa02802 1194 GB_EST24:AI223401 169 AI223401 qg48g01.x1 Soares_testis_NHT Homo sapiens cDNA clone IMAGE:1838448 Homo sapiens 40,828 27-OCT-1998 3′ similar to WP:C25D7.8 CE08394;, mRNA sequence. GB_EST24:AI223401 169 AI223401 qg48g01.x1 Soares_testis_NHT Homo sapiens cDNA clone IMAGE:1838448 Homo sapiens 40,828 27-OCT-1998 3′ similar to WP:C25D7.8 CE08394;, mRNA sequence. rxa02814 494 GB_BA1:MTCY7D11 22070 Z95120 Mycobacterium tuberculosis H37Rv complete genome; segment 138/162. Mycobacterium tuberculosis 58,418 17-Jun-98 GB_BA1:MTCY7D11 22070 Z95120 Mycobacterium tuberculosis H37Rv complete genome; segment 138/162. Mycobacterium tuberculosis 40,496 17-Jun-98 GB_PR1:HSAJ2962 778 AJ002962 Homo sapiens mRNA for hB-FABP. Homo sapiens 39,826 8-Jan-98 rxa02843 608 GB_BA1:CGAJ4934 1160 AJ004934 Corynebacterium glutamicum dapD gene, complete CDS. Corynebacterium glutamicum 100,000 17-Jun-98 GB_BA1:MTCI364 29540 Z93777 Mycobacterium tuberculosis H37Rv complete genome; segment 52/162. Mycobacterium tuberculosis 37,710 17-Jun-98 GB_BA1:MLU15180 38675 U15180 Mycobacterium leprae cosmid B1756. Mycobacterium leprae 39,626 09-MAR-1995 rxs03205 963 GB_BA1:BLSIGBGN 2906 Z49824 B. lactofermentum orf1 gene and sigB gene. Corynebacterium glutamicum 98,854 25-Apr-96 GB_EST21:AA980237 377 AA980237 ua32a12.r1 Soares_mammary_gland_NbMMG Mus musculus cDNA clone Mus musculus 41,489 27-MAY-1998 IMAGE:1348414 5′ similar to TR:Q61025 Q61025 HYPOTHETICAL 15.2 KD PROTEIN.;, mRNA sequence. GB_EST23:AI158316 371 AI158316 ud27c05.r1 Soares_thymus_2NbMT Mus musculus cDNA clone Mus musculus 38,005 30-Sep-98 IMAGE:1447112 5′, mRNA sequence. rxs03223 1237 GB_IN1:LMFL2743 38368 AL031910 Leishmania major Friedlin chromosome 4 cosmid L2743. Leishmania major 39,869 15-DEC-1999 GB_PR3:HSDJ61B2 119666 AL096710 Human DNA sequence from clone RP1-61B2 on chromosome 6p11.2-12.3 Homo sapiens 34,930 17-DEC-1999 Contains isoforms 1 and 3 of BPAG1 (bullous pemphigoid antigen 1 (230/240kD), an exon of a gene similar to murine MACF cytoskeletal protein, STSs and GSSs, complete sequence. GB_PR3:HSDJ61B2 119666 AL096710 Human DNA sequence from clone RP1-61B2 on chromosome 6p11.2-12.3 Homo sapiens 34,634 17-DEC-1999 Contains isoforms 1 and 3 of BPAG1 (bullous pemphigoid antigen 1 (230/240kD), an exon of a gene similar to murine MACF cytoskeletal protein, STSs and GSSs, complete sequence.

[0230]

1 125 1 1840 DNA Corynebacterium glutamicum CDS (363)..(1676) 1 cagaaactgt gtgcagaaat gcatgcagaa aaaggaaagt tcgggccaag atgggtgttt 60 ctgtatgccg atgatcggat ctttgacagc tgggtatgcg acaaatcacc gagagttgtt 120 aattcttaac aatggaaaag taacattgag agatgattta taccatcctg caccatttag 180 agtggggcta gtcatacccc cataacccta gctgtacgca atcgatttca aatcagttgg 240 aaaaagtcaa gaaaattacc cgagaattaa tttataccac acagtctatt gcaatagacc 300 aagctgttca gtagggtgca tgggagaaga atttcctaat aaaaactctt aaggacctcc 360 aa atg cca aag tac gac aat tcc aat gct gac cag tgg ggc ttt gaa 407 Met Pro Lys Tyr Asp Asn Ser Asn Ala Asp Gln Trp Gly Phe Glu 1 5 10 15 acc cgc tcc att cac gca ggc cag tca gta gac gca cag acc agc gca 455 Thr Arg Ser Ile His Ala Gly Gln Ser Val Asp Ala Gln Thr Ser Ala 20 25 30 cga aac ctt ccg atc tac caa tcc acc gct ttc gtg ttc gac tcc gct 503 Arg Asn Leu Pro Ile Tyr Gln Ser Thr Ala Phe Val Phe Asp Ser Ala 35 40 45 gag cac gcc aag cag cgt ttc gca ctt gag gat cta ggc cct gtt tac 551 Glu His Ala Lys Gln Arg Phe Ala Leu Glu Asp Leu Gly Pro Val Tyr 50 55 60 tcc cgc ctc acc aac cca acc gtt gag gct ttg gaa aac cgc atc gct 599 Ser Arg Leu Thr Asn Pro Thr Val Glu Ala Leu Glu Asn Arg Ile Ala 65 70 75 tcc ctc gaa ggt ggc gtc cac gct gta gcg ttc tcc tcc gga cag gcc 647 Ser Leu Glu Gly Gly Val His Ala Val Ala Phe Ser Ser Gly Gln Ala 80 85 90 95 gca acc acc aac gcc att ttg aac ctg gca gga gcg ggc gac cac atc 695 Ala Thr Thr Asn Ala Ile Leu Asn Leu Ala Gly Ala Gly Asp His Ile 100 105 110 gtc acc tcc cca cgc ctc tac ggt ggc acc gag act cta ttc ctt atc 743 Val Thr Ser Pro Arg Leu Tyr Gly Gly Thr Glu Thr Leu Phe Leu Ile 115 120 125 act ctt aac cgc ctg ggt atc gat gtt tcc ttc gtg gaa aac ccc gac 791 Thr Leu Asn Arg Leu Gly Ile Asp Val Ser Phe Val Glu Asn Pro Asp 130 135 140 gac cct gag tcc tgg cag gca gcc gtt cag cca aac acc aaa gca ttc 839 Asp Pro Glu Ser Trp Gln Ala Ala Val Gln Pro Asn Thr Lys Ala Phe 145 150 155 ttc ggc gag act ttc gcc aac cca cag gca gac gtc ctg gat att cct 887 Phe Gly Glu Thr Phe Ala Asn Pro Gln Ala Asp Val Leu Asp Ile Pro 160 165 170 175 gcg gtg gct gaa gtt gcg cac cgc aac agc gtt cca ctg atc atc gac 935 Ala Val Ala Glu Val Ala His Arg Asn Ser Val Pro Leu Ile Ile Asp 180 185 190 aac acc atc gct acc gca gcg ctc gtg cgc ccg ctc gag ctc ggc gca 983 Asn Thr Ile Ala Thr Ala Ala Leu Val Arg Pro Leu Glu Leu Gly Ala 195 200 205 gac gtt gtc gtc gct tcc ctc acc aag ttc tac acc ggc aac ggc tcc 1031 Asp Val Val Val Ala Ser Leu Thr Lys Phe Tyr Thr Gly Asn Gly Ser 210 215 220 gga ctg ggc ggc gtg ctt atc gac ggc gga aag ttc gat tgg act gtc 1079 Gly Leu Gly Gly Val Leu Ile Asp Gly Gly Lys Phe Asp Trp Thr Val 225 230 235 gaa aag gat gga aag cca gta ttc ccc tac ttc gtc act cca gat gct 1127 Glu Lys Asp Gly Lys Pro Val Phe Pro Tyr Phe Val Thr Pro Asp Ala 240 245 250 255 gct tac cac gga ttg aag tac gca gac ctt ggt gca cca gcc ttc ggc 1175 Ala Tyr His Gly Leu Lys Tyr Ala Asp Leu Gly Ala Pro Ala Phe Gly 260 265 270 ctc aag gtt cgc gtt ggc ctt cta cgc gac acc ggc tcc acc ctc tcc 1223 Leu Lys Val Arg Val Gly Leu Leu Arg Asp Thr Gly Ser Thr Leu Ser 275 280 285 gca ttc aac gca tgg gct gca gtc cag ggc atc gac acc ctt tcc ctg 1271 Ala Phe Asn Ala Trp Ala Ala Val Gln Gly Ile Asp Thr Leu Ser Leu 290 295 300 cgc ctg gag cgc cac aac gaa aac gcc atc aag gtt gca gaa ttc ctc 1319 Arg Leu Glu Arg His Asn Glu Asn Ala Ile Lys Val Ala Glu Phe Leu 305 310 315 aac aac cac gag aag gtg gaa aag gtt aac ttc gca ggc ctg aag gat 1367 Asn Asn His Glu Lys Val Glu Lys Val Asn Phe Ala Gly Leu Lys Asp 320 325 330 335 tcc cct tgg tac gca acc aag gaa aag ctt ggc ctg aag tac acc ggc 1415 Ser Pro Trp Tyr Ala Thr Lys Glu Lys Leu Gly Leu Lys Tyr Thr Gly 340 345 350 tcc gtt ctc acc ttc gag atc aag ggc ggc aag gat gag gct tgg gca 1463 Ser Val Leu Thr Phe Glu Ile Lys Gly Gly Lys Asp Glu Ala Trp Ala 355 360 365 ttt atc gac gcc ctg aag cta cac tcc aac ctt gca aac atc ggc gat 1511 Phe Ile Asp Ala Leu Lys Leu His Ser Asn Leu Ala Asn Ile Gly Asp 370 375 380 gtt cgc tcc ctc gtt gtt cac cca gca acc acc acc cat tca cag tcc 1559 Val Arg Ser Leu Val Val His Pro Ala Thr Thr Thr His Ser Gln Ser 385 390 395 gac gaa gct ggc ctg gca cgc gcg ggc gtt acc cag tcc acc gtc cgc 1607 Asp Glu Ala Gly Leu Ala Arg Ala Gly Val Thr Gln Ser Thr Val Arg 400 405 410 415 ctg tcc gtt ggc atc gag acc att gat gat atc atc gct gac ctc gaa 1655 Leu Ser Val Gly Ile Glu Thr Ile Asp Asp Ile Ile Ala Asp Leu Glu 420 425 430 ggc ggc ttt gct gca atc tag ctttaaatag actcacccca gtgcttaaag 1706 Gly Gly Phe Ala Ala Ile 435 cgctgggttt ttctttttca gactcgtgag aatgcaaact agactagaca gagctgtcca 1766 tatacactgg acgaagtttt agtcttgtcc acccagaaca ggcggttatt ttcatgccca 1826 ccctcgcgcc ttca 1840 2 437 PRT Corynebacterium glutamicum 2 Met Pro Lys Tyr Asp Asn Ser Asn Ala Asp Gln Trp Gly Phe Glu Thr 1 5 10 15 Arg Ser Ile His Ala Gly Gln Ser Val Asp Ala Gln Thr Ser Ala Arg 20 25 30 Asn Leu Pro Ile Tyr Gln Ser Thr Ala Phe Val Phe Asp Ser Ala Glu 35 40 45 His Ala Lys Gln Arg Phe Ala Leu Glu Asp Leu Gly Pro Val Tyr Ser 50 55 60 Arg Leu Thr Asn Pro Thr Val Glu Ala Leu Glu Asn Arg Ile Ala Ser 65 70 75 80 Leu Glu Gly Gly Val His Ala Val Ala Phe Ser Ser Gly Gln Ala Ala 85 90 95 Thr Thr Asn Ala Ile Leu Asn Leu Ala Gly Ala Gly Asp His Ile Val 100 105 110 Thr Ser Pro Arg Leu Tyr Gly Gly Thr Glu Thr Leu Phe Leu Ile Thr 115 120 125 Leu Asn Arg Leu Gly Ile Asp Val Ser Phe Val Glu Asn Pro Asp Asp 130 135 140 Pro Glu Ser Trp Gln Ala Ala Val Gln Pro Asn Thr Lys Ala Phe Phe 145 150 155 160 Gly Glu Thr Phe Ala Asn Pro Gln Ala Asp Val Leu Asp Ile Pro Ala 165 170 175 Val Ala Glu Val Ala His Arg Asn Ser Val Pro Leu Ile Ile Asp Asn 180 185 190 Thr Ile Ala Thr Ala Ala Leu Val Arg Pro Leu Glu Leu Gly Ala Asp 195 200 205 Val Val Val Ala Ser Leu Thr Lys Phe Tyr Thr Gly Asn Gly Ser Gly 210 215 220 Leu Gly Gly Val Leu Ile Asp Gly Gly Lys Phe Asp Trp Thr Val Glu 225 230 235 240 Lys Asp Gly Lys Pro Val Phe Pro Tyr Phe Val Thr Pro Asp Ala Ala 245 250 255 Tyr His Gly Leu Lys Tyr Ala Asp Leu Gly Ala Pro Ala Phe Gly Leu 260 265 270 Lys Val Arg Val Gly Leu Leu Arg Asp Thr Gly Ser Thr Leu Ser Ala 275 280 285 Phe Asn Ala Trp Ala Ala Val Gln Gly Ile Asp Thr Leu Ser Leu Arg 290 295 300 Leu Glu Arg His Asn Glu Asn Ala Ile Lys Val Ala Glu Phe Leu Asn 305 310 315 320 Asn His Glu Lys Val Glu Lys Val Asn Phe Ala Gly Leu Lys Asp Ser 325 330 335 Pro Trp Tyr Ala Thr Lys Glu Lys Leu Gly Leu Lys Tyr Thr Gly Ser 340 345 350 Val Leu Thr Phe Glu Ile Lys Gly Gly Lys Asp Glu Ala Trp Ala Phe 355 360 365 Ile Asp Ala Leu Lys Leu His Ser Asn Leu Ala Asn Ile Gly Asp Val 370 375 380 Arg Ser Leu Val Val His Pro Ala Thr Thr Thr His Ser Gln Ser Asp 385 390 395 400 Glu Ala Gly Leu Ala Arg Ala Gly Val Thr Gln Ser Thr Val Arg Leu 405 410 415 Ser Val Gly Ile Glu Thr Ile Asp Asp Ile Ile Ala Asp Leu Glu Gly 420 425 430 Gly Phe Ala Ala Ile 435 3 1495 DNA Corynebacterium glutamicum CDS (287)..(1264) 3 ccatggtttc ctcagcggaa acggcttggc tatcagcact ttcacccgaa cagcctgcaa 60 gaagtgcgac ggctaacagg gctgggattg tcctcaactt cacttcgggc tccttcttag 120 taataggttc gtagaaaagt ttactagcct agagagtatg cgatttcctg aactcgaaga 180 attgaagaat cgccggacct tgaaatggac ccggtttcca gaagacgtgc ttcctttgtg 240 ggttgcggaa agtgattttg gcacctgccc gcagttgaag gaagct atg gca gat 295 Met Ala Asp 1 gcc gtt gag cgc gag gtc ttc gga tac cca cca gat gct act ggg ttg 343 Ala Val Glu Arg Glu Val Phe Gly Tyr Pro Pro Asp Ala Thr Gly Leu 5 10 15 aat gat gcg ttg act gga ttc tac gag cgt cgc tat ggg ttt ggc cca 391 Asn Asp Ala Leu Thr Gly Phe Tyr Glu Arg Arg Tyr Gly Phe Gly Pro 20 25 30 35 aat ccg gaa agt gtt ttc gcc att ccg gat gtg gtt cgt ggc ctg aag 439 Asn Pro Glu Ser Val Phe Ala Ile Pro Asp Val Val Arg Gly Leu Lys 40 45 50 ctt gcc att gag cat ttc act aag cct ggt tcg gcg atc att gtg ccg 487 Leu Ala Ile Glu His Phe Thr Lys Pro Gly Ser Ala Ile Ile Val Pro 55 60 65 ttg cct gca tac cct cct ttc att gag ttg cct aag gtg act ggt cgt 535 Leu Pro Ala Tyr Pro Pro Phe Ile Glu Leu Pro Lys Val Thr Gly Arg 70 75 80 cag gcg atc tac att gat gcg cat gag tac gat ttg aag gaa att gag 583 Gln Ala Ile Tyr Ile Asp Ala His Glu Tyr Asp Leu Lys Glu Ile Glu 85 90 95 aag gcc ttc gct gac ggt gcg gga tca ctg ttg ttc tgc aat cca cac 631 Lys Ala Phe Ala Asp Gly Ala Gly Ser Leu Leu Phe Cys Asn Pro His 100 105 110 115 aac cca ctg ggc acg gtc ttt tct gaa gag tac atc cgc gag ctc acc 679 Asn Pro Leu Gly Thr Val Phe Ser Glu Glu Tyr Ile Arg Glu Leu Thr 120 125 130 gat att gcg gcg aag tac gat gcc cgc atc atc gtc gat gag atc cac 727 Asp Ile Ala Ala Lys Tyr Asp Ala Arg Ile Ile Val Asp Glu Ile His 135 140 145 gcg cca ctg gtt tat gaa ggc acc cat gtg gtt gct gct ggt gtt tct 775 Ala Pro Leu Val Tyr Glu Gly Thr His Val Val Ala Ala Gly Val Ser 150 155 160 gag aac gct gca aac act tgc atc acc atc acc gca act tct aag gcg 823 Glu Asn Ala Ala Asn Thr Cys Ile Thr Ile Thr Ala Thr Ser Lys Ala 165 170 175 tgg aac act gct ggt ttg aag tgt gct cag atc ttc ttc agt aat gaa 871 Trp Asn Thr Ala Gly Leu Lys Cys Ala Gln Ile Phe Phe Ser Asn Glu 180 185 190 195 gcc gat gtg aag gcc tgg aag aat ttg tcg gat att acc cgt gac ggt 919 Ala Asp Val Lys Ala Trp Lys Asn Leu Ser Asp Ile Thr Arg Asp Gly 200 205 210 gtg tcc atc ctt gga ttg atc gct gcg gag aca gtg tac aac gag ggc 967 Val Ser Ile Leu Gly Leu Ile Ala Ala Glu Thr Val Tyr Asn Glu Gly 215 220 225 gaa gaa ttc ctt gat gag tca att cag att ctc aag gac aac cgt gac 1015 Glu Glu Phe Leu Asp Glu Ser Ile Gln Ile Leu Lys Asp Asn Arg Asp 230 235 240 ttt gcg gct gct gaa ctg gaa aag ctt ggc gtg aag gtc tac gca ccg 1063 Phe Ala Ala Ala Glu Leu Glu Lys Leu Gly Val Lys Val Tyr Ala Pro 245 250 255 gac tcc act tat ttg atg tgg ttg gac ttc gct ggc acc aag atc gaa 1111 Asp Ser Thr Tyr Leu Met Trp Leu Asp Phe Ala Gly Thr Lys Ile Glu 260 265 270 275 gag gcg cct tct aaa att ctt cgt gag gag ggt aag gtc atg ctg aat 1159 Glu Ala Pro Ser Lys Ile Leu Arg Glu Glu Gly Lys Val Met Leu Asn 280 285 290 gat ggc gca gct ttt ggt ggt ttc acc acc tgc gct cgt ctt aat ttt 1207 Asp Gly Ala Ala Phe Gly Gly Phe Thr Thr Cys Ala Arg Leu Asn Phe 295 300 305 gcg tgt tcc aga gag acc ctt gag gag ggg ctg cgc cgt atc gcc agc 1255 Ala Cys Ser Arg Glu Thr Leu Glu Glu Gly Leu Arg Arg Ile Ala Ser 310 315 320 gtg ttg taa ataatgagta aaaagtctgt cctgattact tctttgatgc 1304 Val Leu 325 tgttttccat gttcttcgga gctggaaacc tcatcttccc gccgatgctt ggattgtcgg 1364 caggaaccaa ctatctacca gctatcttag gatttctagc aacgagtgtt ctgctcccgg 1424 tgctggcgat tatcgcggtg gtgttgtcgg gagaaaatgt caaggacatg gcttctcgtg 1484 gcggtaagat c 1495 4 325 PRT Corynebacterium glutamicum 4 Met Ala Asp Ala Val Glu Arg Glu Val Phe Gly Tyr Pro Pro Asp Ala 1 5 10 15 Thr Gly Leu Asn Asp Ala Leu Thr Gly Phe Tyr Glu Arg Arg Tyr Gly 20 25 30 Phe Gly Pro Asn Pro Glu Ser Val Phe Ala Ile Pro Asp Val Val Arg 35 40 45 Gly Leu Lys Leu Ala Ile Glu His Phe Thr Lys Pro Gly Ser Ala Ile 50 55 60 Ile Val Pro Leu Pro Ala Tyr Pro Pro Phe Ile Glu Leu Pro Lys Val 65 70 75 80 Thr Gly Arg Gln Ala Ile Tyr Ile Asp Ala His Glu Tyr Asp Leu Lys 85 90 95 Glu Ile Glu Lys Ala Phe Ala Asp Gly Ala Gly Ser Leu Leu Phe Cys 100 105 110 Asn Pro His Asn Pro Leu Gly Thr Val Phe Ser Glu Glu Tyr Ile Arg 115 120 125 Glu Leu Thr Asp Ile Ala Ala Lys Tyr Asp Ala Arg Ile Ile Val Asp 130 135 140 Glu Ile His Ala Pro Leu Val Tyr Glu Gly Thr His Val Val Ala Ala 145 150 155 160 Gly Val Ser Glu Asn Ala Ala Asn Thr Cys Ile Thr Ile Thr Ala Thr 165 170 175 Ser Lys Ala Trp Asn Thr Ala Gly Leu Lys Cys Ala Gln Ile Phe Phe 180 185 190 Ser Asn Glu Ala Asp Val Lys Ala Trp Lys Asn Leu Ser Asp Ile Thr 195 200 205 Arg Asp Gly Val Ser Ile Leu Gly Leu Ile Ala Ala Glu Thr Val Tyr 210 215 220 Asn Glu Gly Glu Glu Phe Leu Asp Glu Ser Ile Gln Ile Leu Lys Asp 225 230 235 240 Asn Arg Asp Phe Ala Ala Ala Glu Leu Glu Lys Leu Gly Val Lys Val 245 250 255 Tyr Ala Pro Asp Ser Thr Tyr Leu Met Trp Leu Asp Phe Ala Gly Thr 260 265 270 Lys Ile Glu Glu Ala Pro Ser Lys Ile Leu Arg Glu Glu Gly Lys Val 275 280 285 Met Leu Asn Asp Gly Ala Ala Phe Gly Gly Phe Thr Thr Cys Ala Arg 290 295 300 Leu Asn Phe Ala Cys Ser Arg Glu Thr Leu Glu Glu Gly Leu Arg Arg 305 310 315 320 Ile Ala Ser Val Leu 325 5 1033 DNA Corynebacterium glutamicum CDS (101)..(1006) 5 gtgcggatcg ggtatccgcg ctacacttag aggtgttaga gatcatgagt ttccacgaac 60 tgtaacgcag gattcaccaa tcaatgaaag gtcgaccgac atg agc act gaa gac 115 Met Ser Thr Glu Asp 1 5 att gtc gtc gta gca gta gat ggc tcg gac gcc tca aaa caa gct gtt 163 Ile Val Val Val Ala Val Asp Gly Ser Asp Ala Ser Lys Gln Ala Val 10 15 20 cgg tgg gct gca aat acc gcc aac aaa cgt ggc att cca ctt cgc ttg 211 Arg Trp Ala Ala Asn Thr Ala Asn Lys Arg Gly Ile Pro Leu Arg Leu 25 30 35 gct tcc agc tac acc atg cct cag ttc ctc tac gca gag gga atg gtt 259 Ala Ser Ser Tyr Thr Met Pro Gln Phe Leu Tyr Ala Glu Gly Met Val 40 45 50 cca cca caa gag ctt ttc gat gac ctc cag gcc gaa gcc ctg gaa aag 307 Pro Pro Gln Glu Leu Phe Asp Asp Leu Gln Ala Glu Ala Leu Glu Lys 55 60 65 att aac gaa gcc cgt gac atc gcc cat gag gta gcg cca gaa atc aag 355 Ile Asn Glu Ala Arg Asp Ile Ala His Glu Val Ala Pro Glu Ile Lys 70 75 80 85 atc ggg cac acc atc gct gaa ggc agt ccc atc gac atg ctg ttg gaa 403 Ile Gly His Thr Ile Ala Glu Gly Ser Pro Ile Asp Met Leu Leu Glu 90 95 100 atg tct ccc gat gcc aca atg atc gtc atg ggt tcc cgc gga ctc ggc 451 Met Ser Pro Asp Ala Thr Met Ile Val Met Gly Ser Arg Gly Leu Gly 105 110 115 gga ctc tcc gga atg gtc atg ggc tcc gtc tcc ggt gca gtg gtc agc 499 Gly Leu Ser Gly Met Val Met Gly Ser Val Ser Gly Ala Val Val Ser 120 125 130 cac gca aag tgt cca gtc gtt gtt gtc cgt gaa gac agc gca gtc aac 547 His Ala Lys Cys Pro Val Val Val Val Arg Glu Asp Ser Ala Val Asn 135 140 145 gaa gac agc aag tac ggc cca gtc gtc gtc ggt gtg gat ggc tcc gaa 595 Glu Asp Ser Lys Tyr Gly Pro Val Val Val Gly Val Asp Gly Ser Glu 150 155 160 165 gtc tcc caa cag gca acc gaa tac gca ttt gcg gaa gct gaa gct cgt 643 Val Ser Gln Gln Ala Thr Glu Tyr Ala Phe Ala Glu Ala Glu Ala Arg 170 175 180 ggc gcc gaa ctc gtt gca gtt cac acc tgg atg gac atg cag gta cag 691 Gly Ala Glu Leu Val Ala Val His Thr Trp Met Asp Met Gln Val Gln 185 190 195 gca tca ctt gca ggt ctt gca gct gct caa cag cag tgg gat gaa gtg 739 Ala Ser Leu Ala Gly Leu Ala Ala Ala Gln Gln Gln Trp Asp Glu Val 200 205 210 gaa cgt cag caa acc gac atg ctg atc gaa cgc ctc gca cca ctg gtg 787 Glu Arg Gln Gln Thr Asp Met Leu Ile Glu Arg Leu Ala Pro Leu Val 215 220 225 gaa aag tac cca agt gta acc gtc aag aag atc atc acc cgt gac cgc 835 Glu Lys Tyr Pro Ser Val Thr Val Lys Lys Ile Ile Thr Arg Asp Arg 230 235 240 245 cca gtt cgc gca ctt gca gaa gca tct gaa aac gcg cag ctc cta gtc 883 Pro Val Arg Ala Leu Ala Glu Ala Ser Glu Asn Ala Gln Leu Leu Val 250 255 260 gtt ggt tcc cat ggt cgt ggc gga ttt aag ggc atg ctc ctt ggc tcc 931 Val Gly Ser His Gly Arg Gly Gly Phe Lys Gly Met Leu Leu Gly Ser 265 270 275 acc tcc cgc gca ctg ctg caa tcc gca ccg tgc cca atg atg gtg gtt 979 Thr Ser Arg Ala Leu Leu Gln Ser Ala Pro Cys Pro Met Met Val Val 280 285 290 cgc cca cct gag aag att aag aag tag tttcttttaa gtttcgatgc cccggtt 1033 Arg Pro Pro Glu Lys Ile Lys Lys 295 300 6 301 PRT Corynebacterium glutamicum 6 Met Ser Thr Glu Asp Ile Val Val Val Ala Val Asp Gly Ser Asp Ala 1 5 10 15 Ser Lys Gln Ala Val Arg Trp Ala Ala Asn Thr Ala Asn Lys Arg Gly 20 25 30 Ile Pro Leu Arg Leu Ala Ser Ser Tyr Thr Met Pro Gln Phe Leu Tyr 35 40 45 Ala Glu Gly Met Val Pro Pro Gln Glu Leu Phe Asp Asp Leu Gln Ala 50 55 60 Glu Ala Leu Glu Lys Ile Asn Glu Ala Arg Asp Ile Ala His Glu Val 65 70 75 80 Ala Pro Glu Ile Lys Ile Gly His Thr Ile Ala Glu Gly Ser Pro Ile 85 90 95 Asp Met Leu Leu Glu Met Ser Pro Asp Ala Thr Met Ile Val Met Gly 100 105 110 Ser Arg Gly Leu Gly Gly Leu Ser Gly Met Val Met Gly Ser Val Ser 115 120 125 Gly Ala Val Val Ser His Ala Lys Cys Pro Val Val Val Val Arg Glu 130 135 140 Asp Ser Ala Val Asn Glu Asp Ser Lys Tyr Gly Pro Val Val Val Gly 145 150 155 160 Val Asp Gly Ser Glu Val Ser Gln Gln Ala Thr Glu Tyr Ala Phe Ala 165 170 175 Glu Ala Glu Ala Arg Gly Ala Glu Leu Val Ala Val His Thr Trp Met 180 185 190 Asp Met Gln Val Gln Ala Ser Leu Ala Gly Leu Ala Ala Ala Gln Gln 195 200 205 Gln Trp Asp Glu Val Glu Arg Gln Gln Thr Asp Met Leu Ile Glu Arg 210 215 220 Leu Ala Pro Leu Val Glu Lys Tyr Pro Ser Val Thr Val Lys Lys Ile 225 230 235 240 Ile Thr Arg Asp Arg Pro Val Arg Ala Leu Ala Glu Ala Ser Glu Asn 245 250 255 Ala Gln Leu Leu Val Val Gly Ser His Gly Arg Gly Gly Phe Lys Gly 260 265 270 Met Leu Leu Gly Ser Thr Ser Arg Ala Leu Leu Gln Ser Ala Pro Cys 275 280 285 Pro Met Met Val Val Arg Pro Pro Glu Lys Ile Lys Lys 290 295 300 7 948 DNA Corynebacterium glutamicum CDS (101)..(925) RXA02229 7 gctggttcaa cagagaccac cgcgtgtcct gggtcgacgc ctctggcgat cccaccgcac 60 aagccttgga gattttgggt ctacaatagc gagggtgaat ttg acc atc ccc ttt 115 Leu Thr Ile Pro Phe 1 5 gcc aaa ggc cac gcc acc gaa aac gac ttc atc atc atc ccc gat gag 163 Ala Lys Gly His Ala Thr Glu Asn Asp Phe Ile Ile Ile Pro Asp Glu 10 15 20 gat gcg cgc cta gat tta act cca gaa atg gtg gtc acg ctg tgt gac 211 Asp Ala Arg Leu Asp Leu Thr Pro Glu Met Val Val Thr Leu Cys Asp 25 30 35 cgc cgc gcc ggg atc ggt gct gat ggt atc ctc cgc gtg gtt aaa gct 259 Arg Arg Ala Gly Ile Gly Ala Asp Gly Ile Leu Arg Val Val Lys Ala 40 45 50 gca gac gta gaa ggc tcc acg gtc gac cca tcg ctg tgg ttc atg gat 307 Ala Asp Val Glu Gly Ser Thr Val Asp Pro Ser Leu Trp Phe Met Asp 55 60 65 tac cgc aac gcc gat gga tct ttg gct gaa atg tgc ggc aat ggt gtg 355 Tyr Arg Asn Ala Asp Gly Ser Leu Ala Glu Met Cys Gly Asn Gly Val 70 75 80 85 cgc ctg ttc gcg cac tgg ctg tac tcc cgc ggt ctt gtt gat aat acg 403 Arg Leu Phe Ala His Trp Leu Tyr Ser Arg Gly Leu Val Asp Asn Thr 90 95 100 agc ttt gat atc ggt acc cgc gcc ggt gtc cgc cac gtt gat att ttg 451 Ser Phe Asp Ile Gly Thr Arg Ala Gly Val Arg His Val Asp Ile Leu 105 110 115 cag gca gat caa cat tct gcg cag gtc cgc gtt gat atg ggc atc cct 499 Gln Ala Asp Gln His Ser Ala Gln Val Arg Val Asp Met Gly Ile Pro 120 125 130 gac gtc acg gga tta tcc acc tgc gac atc aac ggc caa gta ttc gct 547 Asp Val Thr Gly Leu Ser Thr Cys Asp Ile Asn Gly Gln Val Phe Ala 135 140 145 ggc ctt ggc gtt gat atg ggt aac cca cac cta gcg tgc gtt gtg ccg 595 Gly Leu Gly Val Asp Met Gly Asn Pro His Leu Ala Cys Val Val Pro 150 155 160 165 ggc tta agt gcg tcg gct ctt gcc gat atg gaa ctg cgc gca cct acg 643 Gly Leu Ser Ala Ser Ala Leu Ala Asp Met Glu Leu Arg Ala Pro Thr 170 175 180 ttt gat cag gaa ttc ttc ccc cac ggt gtg aac gta gaa atc gtc aca 691 Phe Asp Gln Glu Phe Phe Pro His Gly Val Asn Val Glu Ile Val Thr 185 190 195 gaa tta gaa gat gac gca gta tcg atg cgc gtg tgg gaa cgc gga gtg 739 Glu Leu Glu Asp Asp Ala Val Ser Met Arg Val Trp Glu Arg Gly Val 200 205 210 ggc gaa acc cgc tcc tgt ggc acg gga acc gtt gct gca gcg tgt gct 787 Gly Glu Thr Arg Ser Cys Gly Thr Gly Thr Val Ala Ala Ala Cys Ala 215 220 225 gct tta gct gat gct gga ttg gga gaa ggc aca gct aaa gtg tgc gtt 835 Ala Leu Ala Asp Ala Gly Leu Gly Glu Gly Thr Ala Lys Val Cys Val 230 235 240 245 cca cgt ggg gaa gta gaa gtc cag atc ttt gac gac ggc tcc aca ctc 883 Pro Arg Gly Glu Val Glu Val Gln Ile Phe Asp Asp Gly Ser Thr Leu 250 255 260 acc ggc cca agc gcc atc atc gca ctc ggt gag gtg cag atc 925 Thr Gly Pro Ser Ala Ile Ile Ala Leu Gly Glu Val Gln Ile 265 270 275 taagattcgc gattgtagtt cgg 948 8 275 PRT Corynebacterium glutamicum 8 Leu Thr Ile Pro Phe Ala Lys Gly His Ala Thr Glu Asn Asp Phe Ile 1 5 10 15 Ile Ile Pro Asp Glu Asp Ala Arg Leu Asp Leu Thr Pro Glu Met Val 20 25 30 Val Thr Leu Cys Asp Arg Arg Ala Gly Ile Gly Ala Asp Gly Ile Leu 35 40 45 Arg Val Val Lys Ala Ala Asp Val Glu Gly Ser Thr Val Asp Pro Ser 50 55 60 Leu Trp Phe Met Asp Tyr Arg Asn Ala Asp Gly Ser Leu Ala Glu Met 65 70 75 80 Cys Gly Asn Gly Val Arg Leu Phe Ala His Trp Leu Tyr Ser Arg Gly 85 90 95 Leu Val Asp Asn Thr Ser Phe Asp Ile Gly Thr Arg Ala Gly Val Arg 100 105 110 His Val Asp Ile Leu Gln Ala Asp Gln His Ser Ala Gln Val Arg Val 115 120 125 Asp Met Gly Ile Pro Asp Val Thr Gly Leu Ser Thr Cys Asp Ile Asn 130 135 140 Gly Gln Val Phe Ala Gly Leu Gly Val Asp Met Gly Asn Pro His Leu 145 150 155 160 Ala Cys Val Val Pro Gly Leu Ser Ala Ser Ala Leu Ala Asp Met Glu 165 170 175 Leu Arg Ala Pro Thr Phe Asp Gln Glu Phe Phe Pro His Gly Val Asn 180 185 190 Val Glu Ile Val Thr Glu Leu Glu Asp Asp Ala Val Ser Met Arg Val 195 200 205 Trp Glu Arg Gly Val Gly Glu Thr Arg Ser Cys Gly Thr Gly Thr Val 210 215 220 Ala Ala Ala Cys Ala Ala Leu Ala Asp Ala Gly Leu Gly Glu Gly Thr 225 230 235 240 Ala Lys Val Cys Val Pro Arg Gly Glu Val Glu Val Gln Ile Phe Asp 245 250 255 Asp Gly Ser Thr Leu Thr Gly Pro Ser Ala Ile Ile Ala Leu Gly Glu 260 265 270 Val Gln Ile 275 9 1491 DNA Corynebacterium glutamicum CDS (101)..(1468) RXS02970 9 aaccgacaaa acagccgttc acgtgctaaa gcagctcggc ttgatctagg gtgaggtgag 60 ttatttaaag acttcataat attttgggga gtgaactggt ttg gca ttg aag ggt 115 Leu Ala Leu Lys Gly 1 5 tac acc aac ttt gac ggt gaa ttc atc gaa ttc gga tct gtg caa gca 163 Tyr Thr Asn Phe Asp Gly Glu Phe Ile Glu Phe Gly Ser Val Gln Ala 10 15 20 aaa gaa gag gaa aaa cgg gca ttc gac aac gat cgc gcg cac gtt ttc 211 Lys Glu Glu Glu Lys Arg Ala Phe Asp Asn Asp Arg Ala His Val Phe 25 30 35 cac tcc tgg tcc gcg cag gac aaa atc agc ccc aaa gta tgg gca gct 259 His Ser Trp Ser Ala Gln Asp Lys Ile Ser Pro Lys Val Trp Ala Ala 40 45 50 gcc gaa ggt tcc acg ctg tac gac ttc gac ggc aac gcc ttc atc gac 307 Ala Glu Gly Ser Thr Leu Tyr Asp Phe Asp Gly Asn Ala Phe Ile Asp 55 60 65 atg ggt tcc caa ctt gtc tcg gca aac tta ggc cac aac aac cct cga 355 Met Gly Ser Gln Leu Val Ser Ala Asn Leu Gly His Asn Asn Pro Arg 70 75 80 85 tta gtt gag gcg atc cag cgc caa gca gcc cgg ttg acc aac atc aac 403 Leu Val Glu Ala Ile Gln Arg Gln Ala Ala Arg Leu Thr Asn Ile Asn 90 95 100 ccg gcc ttc ggc aat gat gtg cgc tct gat gtt gct gca aag atc gtg 451 Pro Ala Phe Gly Asn Asp Val Arg Ser Asp Val Ala Ala Lys Ile Val 105 110 115 tcg atg gcc cgt ggc gaa ttc tcc cac gtg ttt ttc acc aac ggc ggc 499 Ser Met Ala Arg Gly Glu Phe Ser His Val Phe Phe Thr Asn Gly Gly 120 125 130 gcc gac gcc atc gag cac tcc atc cgc atg gct cgc ctg cac acc gga 547 Ala Asp Ala Ile Glu His Ser Ile Arg Met Ala Arg Leu His Thr Gly 135 140 145 cgc aac aaa att ctg tcc gca tac cgc agc tac cac ggc gca acc gga 595 Arg Asn Lys Ile Leu Ser Ala Tyr Arg Ser Tyr His Gly Ala Thr Gly 150 155 160 165 tcc gcg atg atg ctc acc ggc gaa cac cgc cgc ctg ggc aac ccc acc 643 Ser Ala Met Met Leu Thr Gly Glu His Arg Arg Leu Gly Asn Pro Thr 170 175 180 acc gac cca gat atc tac cac ttc tgg gca cca ttc ctg cac cac tcc 691 Thr Asp Pro Asp Ile Tyr His Phe Trp Ala Pro Phe Leu His His Ser 185 190 195 tca ttc ttt gcc acc acc caa gaa gaa gaa tgc gaa cgc gca ctc aag 739 Ser Phe Phe Ala Thr Thr Gln Glu Glu Glu Cys Glu Arg Ala Leu Lys 200 205 210 cac ttg gaa gat gtc atc gcg ttt gaa ggt gct ggc atg atc gca gcg 787 His Leu Glu Asp Val Ile Ala Phe Glu Gly Ala Gly Met Ile Ala Ala 215 220 225 atc gtc ctg gag cca gtg gtg gga tca tca gga atc atc ctg cca cca 835 Ile Val Leu Glu Pro Val Val Gly Ser Ser Gly Ile Ile Leu Pro Pro 230 235 240 245 gca ggt tac tta aat ggc gtg cgc gaa ctt tgc aac aag cac ggc atc 883 Ala Gly Tyr Leu Asn Gly Val Arg Glu Leu Cys Asn Lys His Gly Ile 250 255 260 ctc ttc atc gcc gac gaa gtc atg gtc gga ttc gga cgc acc gga aaa 931 Leu Phe Ile Ala Asp Glu Val Met Val Gly Phe Gly Arg Thr Gly Lys 265 270 275 ctg ttt gct tac gag cat gct ggc gac gat ttc cag cca gac atg atc 979 Leu Phe Ala Tyr Glu His Ala Gly Asp Asp Phe Gln Pro Asp Met Ile 280 285 290 acc ttc gcc aag ggt gtt aac gca ggt tac gcc cca ctc ggt ggc atc 1027 Thr Phe Ala Lys Gly Val Asn Ala Gly Tyr Ala Pro Leu Gly Gly Ile 295 300 305 gtg atg acc caa tca atc cgc gat acc ttc gga tca gag gca tac tcc 1075 Val Met Thr Gln Ser Ile Arg Asp Thr Phe Gly Ser Glu Ala Tyr Ser 310 315 320 325 ggc gga ctc acc tac tcc gga cac cca ctt gca gta gca ccc gcc aag 1123 Gly Gly Leu Thr Tyr Ser Gly His Pro Leu Ala Val Ala Pro Ala Lys 330 335 340 gca gcg ctg gag att tac gcg gaa gga gag atc att cca cgc gta gct 1171 Ala Ala Leu Glu Ile Tyr Ala Glu Gly Glu Ile Ile Pro Arg Val Ala 345 350 355 cga ctt ggc gct gaa ctg atc gaa cct cgc ctt cgt gaa cta gcg gaa 1219 Arg Leu Gly Ala Glu Leu Ile Glu Pro Arg Leu Arg Glu Leu Ala Glu 360 365 370 gaa aac gta gcg atc gct gac gtg cgg ggc atc gga ttc ttc tgg gca 1267 Glu Asn Val Ala Ile Ala Asp Val Arg Gly Ile Gly Phe Phe Trp Ala 375 380 385 gtg gag ttc aat gca gac gcc act gcc atg gct gcc ggt gct gca gaa 1315 Val Glu Phe Asn Ala Asp Ala Thr Ala Met Ala Ala Gly Ala Ala Glu 390 395 400 405 ttc aag gaa cgc ggc gtg tgg ccg atg atc tcc ggc aac cga ttc cac 1363 Phe Lys Glu Arg Gly Val Trp Pro Met Ile Ser Gly Asn Arg Phe His 410 415 420 atc gcg ccg ccg ctg acc acc act gat gac gaa ttg gta gca ctg ctg 1411 Ile Ala Pro Pro Leu Thr Thr Thr Asp Asp Glu Leu Val Ala Leu Leu 425 430 435 gac gcg gtg gaa gct gca gcc caa gct gtc gag ctg acc ttc gct ggg 1459 Asp Ala Val Glu Ala Ala Ala Gln Ala Val Glu Leu Thr Phe Ala Gly 440 445 450 gcg ttg ttc taagttttct agataacaag gcc 1491 Ala Leu Phe 455 11 1330 DNA Corynebacterium glutamicum CDS (101)..(1330) FRXA01009 11 aaccgacaaa acagccgttc acgtgctaaa gcagctcggc ttgatctagg gtgaggtgag 60 ttatttaaag acttcataat attttgggga gtgaactggt ttg gca ttg aag ggt 115 Leu Ala Leu Lys Gly 1 5 tac acc aac ttt gac ggt gaa ttc atc gaa ttc gga tct gtg caa gca 163 Tyr Thr Asn Phe Asp Gly Glu Phe Ile Glu Phe Gly Ser Val Gln Ala 10 15 20 aaa gaa gag gaa aaa cgg gca ttc gac aac gat cgc gcg cac gtt ttc 211 Lys Glu Glu Glu Lys Arg Ala Phe Asp Asn Asp Arg Ala His Val Phe 25 30 35 cac tcc tgg tcc gcg cag gac aaa atc agc ccc aaa gta tgg gca gct 259 His Ser Trp Ser Ala Gln Asp Lys Ile Ser Pro Lys Val Trp Ala Ala 40 45 50 gcc gaa ggt tcc acg ctg tac gac ttc gac ggc aac gcc ttc atc gac 307 Ala Glu Gly Ser Thr Leu Tyr Asp Phe Asp Gly Asn Ala Phe Ile Asp 55 60 65 atg ggt tcc caa ctt gtc tcg gca aac tta ggc cac aac aac cct cga 355 Met Gly Ser Gln Leu Val Ser Ala Asn Leu Gly His Asn Asn Pro Arg 70 75 80 85 tta gtt gag gcg atc cag cgc caa gca gcc cgg ttg acc aac atc aac 403 Leu Val Glu Ala Ile Gln Arg Gln Ala Ala Arg Leu Thr Asn Ile Asn 90 95 100 ccg gcc ttc ggc aat gat gtg cgc tct gat gtt gct gca aag atc gtg 451 Pro Ala Phe Gly Asn Asp Val Arg Ser Asp Val Ala Ala Lys Ile Val 105 110 115 tcg atg gcc cgt ggc gaa ttc tcc cac gtg ttt ttc acc aac ggc ggc 499 Ser Met Ala Arg Gly Glu Phe Ser His Val Phe Phe Thr Asn Gly Gly 120 125 130 gcc gac gcc atc gag cac tcc atc cgc atg gct cgc ctg cac acc gga 547 Ala Asp Ala Ile Glu His Ser Ile Arg Met Ala Arg Leu His Thr Gly 135 140 145 cgc aac aaa att ctg tcc gca tac cgc agc tac cac ggc gca acc gga 595 Arg Asn Lys Ile Leu Ser Ala Tyr Arg Ser Tyr His Gly Ala Thr Gly 150 155 160 165 tcc gcg atg atg ctc acc ggc gaa cac cgc cgc ctg ggc aac ccc acc 643 Ser Ala Met Met Leu Thr Gly Glu His Arg Arg Leu Gly Asn Pro Thr 170 175 180 acc gac cca gat atc tac cac ttc tgg gca cca ttc ctg cac cac tcc 691 Thr Asp Pro Asp Ile Tyr His Phe Trp Ala Pro Phe Leu His His Ser 185 190 195 tca ttc ttt gcc acc acc caa gaa gaa gaa tgc gaa cgc gca ctc aag 739 Ser Phe Phe Ala Thr Thr Gln Glu Glu Glu Cys Glu Arg Ala Leu Lys 200 205 210 cac ttg gaa gat gtc atc gcg ttt gaa ggt gct ggc atg atc gca gcg 787 His Leu Glu Asp Val Ile Ala Phe Glu Gly Ala Gly Met Ile Ala Ala 215 220 225 atc gtc ctg gag cca gtg gtg gga tca tca gga atc atc ctg cca cca 835 Ile Val Leu Glu Pro Val Val Gly Ser Ser Gly Ile Ile Leu Pro Pro 230 235 240 245 gca ggt tac tta aat ggc gtg cgc gaa ctt tgc aac aag cac ggc atc 883 Ala Gly Tyr Leu Asn Gly Val Arg Glu Leu Cys Asn Lys His Gly Ile 250 255 260 ctc ttc atc gcc gac gaa gtc atg gtc gga ttc gga cgc acc gga aaa 931 Leu Phe Ile Ala Asp Glu Val Met Val Gly Phe Gly Arg Thr Gly Lys 265 270 275 ctg ttt gct tac gag cat gct ggc gac gat ttc cag cca gac atg atc 979 Leu Phe Ala Tyr Glu His Ala Gly Asp Asp Phe Gln Pro Asp Met Ile 280 285 290 acc ttc gcc aag ggt gtt aac gca ggt tac gcc cca ctc ggt ggc atc 1027 Thr Phe Ala Lys Gly Val Asn Ala Gly Tyr Ala Pro Leu Gly Gly Ile 295 300 305 gtg atg acc caa tca atc cgc gat acc ttc gga tca gag gca tac tcc 1075 Val Met Thr Gln Ser Ile Arg Asp Thr Phe Gly Ser Glu Ala Tyr Ser 310 315 320 325 ggc gga ctc acc tac tcc gga cac cca ctt gca gta gca ccc gcc aag 1123 Gly Gly Leu Thr Tyr Ser Gly His Pro Leu Ala Val Ala Pro Ala Lys 330 335 340 gca gcg ctg gag att tac gcg gaa gga gag atc att cca cgc gta gct 1171 Ala Ala Leu Glu Ile Tyr Ala Glu Gly Glu Ile Ile Pro Arg Val Ala 345 350 355 cga ctt ggc gct gaa ctg atc gaa cct cgc ctt cgt gaa cta gcg gaa 1219 Arg Leu Gly Ala Glu Leu Ile Glu Pro Arg Leu Arg Glu Leu Ala Glu 360 365 370 gaa aac gta gcg atc gct gac gtg cgg ggc atc gga ttc ttc tgg gca 1267 Glu Asn Val Ala Ile Ala Asp Val Arg Gly Ile Gly Phe Phe Trp Ala 375 380 385 gtg gag ttc aat gca gac gcc act gcc atg gct gcc ggt gct gca gaa 1315 Val Glu Phe Asn Ala Asp Ala Thr Ala Met Ala Ala Gly Ala Ala Glu 390 395 400 405 ttc aag gaa cgc ggc 1330 Phe Lys Glu Arg Gly 410 12 410 PRT Corynebacterium glutamicum 12 Leu Ala Leu Lys Gly Tyr Thr Asn Phe Asp Gly Glu Phe Ile Glu Phe 1 5 10 15 Gly Ser Val Gln Ala Lys Glu Glu Glu Lys Arg Ala Phe Asp Asn Asp 20 25 30 Arg Ala His Val Phe His Ser Trp Ser Ala Gln Asp Lys Ile Ser Pro 35 40 45 Lys Val Trp Ala Ala Ala Glu Gly Ser Thr Leu Tyr Asp Phe Asp Gly 50 55 60 Asn Ala Phe Ile Asp Met Gly Ser Gln Leu Val Ser Ala Asn Leu Gly 65 70 75 80 His Asn Asn Pro Arg Leu Val Glu Ala Ile Gln Arg Gln Ala Ala Arg 85 90 95 Leu Thr Asn Ile Asn Pro Ala Phe Gly Asn Asp Val Arg Ser Asp Val 100 105 110 Ala Ala Lys Ile Val Ser Met Ala Arg Gly Glu Phe Ser His Val Phe 115 120 125 Phe Thr Asn Gly Gly Ala Asp Ala Ile Glu His Ser Ile Arg Met Ala 130 135 140 Arg Leu His Thr Gly Arg Asn Lys Ile Leu Ser Ala Tyr Arg Ser Tyr 145 150 155 160 His Gly Ala Thr Gly Ser Ala Met Met Leu Thr Gly Glu His Arg Arg 165 170 175 Leu Gly Asn Pro Thr Thr Asp Pro Asp Ile Tyr His Phe Trp Ala Pro 180 185 190 Phe Leu His His Ser Ser Phe Phe Ala Thr Thr Gln Glu Glu Glu Cys 195 200 205 Glu Arg Ala Leu Lys His Leu Glu Asp Val Ile Ala Phe Glu Gly Ala 210 215 220 Gly Met Ile Ala Ala Ile Val Leu Glu Pro Val Val Gly Ser Ser Gly 225 230 235 240 Ile Ile Leu Pro Pro Ala Gly Tyr Leu Asn Gly Val Arg Glu Leu Cys 245 250 255 Asn Lys His Gly Ile Leu Phe Ile Ala Asp Glu Val Met Val Gly Phe 260 265 270 Gly Arg Thr Gly Lys Leu Phe Ala Tyr Glu His Ala Gly Asp Asp Phe 275 280 285 Gln Pro Asp Met Ile Thr Phe Ala Lys Gly Val Asn Ala Gly Tyr Ala 290 295 300 Pro Leu Gly Gly Ile Val Met Thr Gln Ser Ile Arg Asp Thr Phe Gly 305 310 315 320 Ser Glu Ala Tyr Ser Gly Gly Leu Thr Tyr Ser Gly His Pro Leu Ala 325 330 335 Val Ala Pro Ala Lys Ala Ala Leu Glu Ile Tyr Ala Glu Gly Glu Ile 340 345 350 Ile Pro Arg Val Ala Arg Leu Gly Ala Glu Leu Ile Glu Pro Arg Leu 355 360 365 Arg Glu Leu Ala Glu Glu Asn Val Ala Ile Ala Asp Val Arg Gly Ile 370 375 380 Gly Phe Phe Trp Ala Val Glu Phe Asn Ala Asp Ala Thr Ala Met Ala 385 390 395 400 Ala Gly Ala Ala Glu Phe Lys Glu Arg Gly 405 410 13 792 DNA Corynebacterium glutamicum CDS (101)..(769) RXC02390 13 gctggtggtg ctgacccata cgctggaact ccaactgctg ttgataccgc caagatgttt 60 ggccgcgagg atctcgtagc tcgcttcgag tcataggccg gtg gag tgg acc gct 115 Val Glu Trp Thr Ala 1 5 ttt ggc acc ctg att ctg ctc aat ttg gtg ggc agt tta tcc ccg ggg 163 Phe Gly Thr Leu Ile Leu Leu Asn Leu Val Gly Ser Leu Ser Pro Gly 10 15 20 cct gat acc ttt ttc ctc ctc cgc tta gcc acc cgc tcc aga gcg cac 211 Pro Asp Thr Phe Phe Leu Leu Arg Leu Ala Thr Arg Ser Arg Ala His 25 30 35 gcg atc gct ggc gtc gcc ggc atc gtc acc gga ctc acg gtg tgg gtg 259 Ala Ile Ala Gly Val Ala Gly Ile Val Thr Gly Leu Thr Val Trp Val 40 45 50 acg ctg acg gtc gtg gga gca gcg gcg ctg ctc acc act tat ccg tcg 307 Thr Leu Thr Val Val Gly Ala Ala Ala Leu Leu Thr Thr Tyr Pro Ser 55 60 65 att ctc gga atc atc cag ctc gtc ggc ggc acg tac cta agc ttc att 355 Ile Leu Gly Ile Ile Gln Leu Val Gly Gly Thr Tyr Leu Ser Phe Ile 70 75 80 85 ggg tac aag ttg ctg cgc tcg gcg tcg aga gag ctt atc gac gcc cgc 403 Gly Tyr Lys Leu Leu Arg Ser Ala Ser Arg Glu Leu Ile Asp Ala Arg 90 95 100 cag ttc cgt ttc aac gcc gat gcc cga cct atc ccg gat gcg gta gaa 451 Gln Phe Arg Phe Asn Ala Asp Ala Arg Pro Ile Pro Asp Ala Val Glu 105 110 115 gca ctg gga acc cgc act cag gta tat cga caa ggt ttg gcc acc aac 499 Ala Leu Gly Thr Arg Thr Gln Val Tyr Arg Gln Gly Leu Ala Thr Asn 120 125 130 ctg tca aac cct aaa gtt gtc atg tac ttc gcg gca att ctg gct ccg 547 Leu Ser Asn Pro Lys Val Val Met Tyr Phe Ala Ala Ile Leu Ala Pro 135 140 145 ttg atg cca gcg cac cca tca ccg gtg ctg gcg ttc tct atc atc gtg 595 Leu Met Pro Ala His Pro Ser Pro Val Leu Ala Phe Ser Ile Ile Val 150 155 160 165 gcg att tta gtg cag acc ttt gtt acc ttc tct gct gtg tgc ctc att 643 Ala Ile Leu Val Gln Thr Phe Val Thr Phe Ser Ala Val Cys Leu Ile 170 175 180 gtc tct acg gag cgt gtg cgc aaa gca atg ctg cgt gca ggt ccc tgg 691 Val Ser Thr Glu Arg Val Arg Lys Ala Met Leu Arg Ala Gly Pro Trp 185 190 195 ttt gac ctg ctt gct ggc gtt gtc ttc ctc gtt gtg ggt gtg act ctg 739 Phe Asp Leu Leu Ala Gly Val Val Phe Leu Val Val Gly Val Thr Leu 200 205 210 ctg tat gaa ggc ctg acc ggt tta ctc ggg taaaggcata aaaaatggct 789 Leu Tyr Glu Gly Leu Thr Gly Leu Leu Gly 215 220 tcc 792 14 223 PRT Corynebacterium glutamicum 14 Val Glu Trp Thr Ala Phe Gly Thr Leu Ile Leu Leu Asn Leu Val Gly 1 5 10 15 Ser Leu Ser Pro Gly Pro Asp Thr Phe Phe Leu Leu Arg Leu Ala Thr 20 25 30 Arg Ser Arg Ala His Ala Ile Ala Gly Val Ala Gly Ile Val Thr Gly 35 40 45 Leu Thr Val Trp Val Thr Leu Thr Val Val Gly Ala Ala Ala Leu Leu 50 55 60 Thr Thr Tyr Pro Ser Ile Leu Gly Ile Ile Gln Leu Val Gly Gly Thr 65 70 75 80 Tyr Leu Ser Phe Ile Gly Tyr Lys Leu Leu Arg Ser Ala Ser Arg Glu 85 90 95 Leu Ile Asp Ala Arg Gln Phe Arg Phe Asn Ala Asp Ala Arg Pro Ile 100 105 110 Pro Asp Ala Val Glu Ala Leu Gly Thr Arg Thr Gln Val Tyr Arg Gln 115 120 125 Gly Leu Ala Thr Asn Leu Ser Asn Pro Lys Val Val Met Tyr Phe Ala 130 135 140 Ala Ile Leu Ala Pro Leu Met Pro Ala His Pro Ser Pro Val Leu Ala 145 150 155 160 Phe Ser Ile Ile Val Ala Ile Leu Val Gln Thr Phe Val Thr Phe Ser 165 170 175 Ala Val Cys Leu Ile Val Ser Thr Glu Arg Val Arg Lys Ala Met Leu 180 185 190 Arg Ala Gly Pro Trp Phe Asp Leu Leu Ala Gly Val Val Phe Leu Val 195 200 205 Val Gly Val Thr Leu Leu Tyr Glu Gly Leu Thr Gly Leu Leu Gly 210 215 220 15 897 DNA Corynebacterium glutamicum CDS (101)..(874) RXC01796 15 atgtaactcg atcaggtgga aatgcccgca aaagtggcgg cggtggccga gggatggccg 60 ttggtgcggc atcggtggcc tgctactagt cgggctcttc ttg ctc ctt ggc ggt 115 Leu Leu Leu Gly Gly 1 5 aac cct gcc gag atc gac cag gtt tta ggt ggc gat caa acc cag atc 163 Asn Pro Ala Glu Ile Asp Gln Val Leu Gly Gly Asp Gln Thr Gln Ile 10 15 20 gag tct gga gag tcc acc gga gcc ggc gac ttt gat cac tgc caa acc 211 Glu Ser Gly Glu Ser Thr Gly Ala Gly Asp Phe Asp His Cys Gln Thr 25 30 35 ggc gca gat gcc aac gcc agt gat gat tgt cgc ctt tac tac acc tca 259 Gly Ala Asp Ala Asn Ala Ser Asp Asp Cys Arg Leu Tyr Tyr Thr Ser 40 45 50 ttc tcc gtc aat gaa atg tgg cag act ttg ctt cca gct cag gct ggt 307 Phe Ser Val Asn Glu Met Trp Gln Thr Leu Leu Pro Ala Gln Ala Gly 55 60 65 atc gaa tac acc gag ccg aca ttg act ctt ttc aaa aac tcc acc caa 355 Ile Glu Tyr Thr Glu Pro Thr Leu Thr Leu Phe Lys Asn Ser Thr Gln 70 75 80 85 acc ggc tgc ggt ttc gct tct gcg tcc act ggg ccg ttt tac tgt ccg 403 Thr Gly Cys Gly Phe Ala Ser Ala Ser Thr Gly Pro Phe Tyr Cys Pro 90 95 100 tca gac caa gat gct tat ttt gac ttg act ttc ttc gat cag atg cgt 451 Ser Asp Gln Asp Ala Tyr Phe Asp Leu Thr Phe Phe Asp Gln Met Arg 105 110 115 cag ttc ggt gca gaa aac gcc ccg ctt gcc cag atg tac atc gtg gcg 499 Gln Phe Gly Ala Glu Asn Ala Pro Leu Ala Gln Met Tyr Ile Val Ala 120 125 130 cac gag tac ggc cac cac gtc caa aac ctc gag ggc aca ctc gga ctg 547 His Glu Tyr Gly His His Val Gln Asn Leu Glu Gly Thr Leu Gly Leu 135 140 145 tcc aat tac aac gat ccg ggc gct gat tcc aac gcc gtc aag atc gag 595 Ser Asn Tyr Asn Asp Pro Gly Ala Asp Ser Asn Ala Val Lys Ile Glu 150 155 160 165 ttg cag gcc gat tgc tac gca ggc att tgg gct aat cac tcc agc gaa 643 Leu Gln Ala Asp Cys Tyr Ala Gly Ile Trp Ala Asn His Ser Ser Glu 170 175 180 ggc ccg gat ccg cta ctc caa ccc atc acc gaa tct gag cta gat tcc 691 Gly Pro Asp Pro Leu Leu Gln Pro Ile Thr Glu Ser Glu Leu Asp Ser 185 190 195 gct ctc ctt gct gca agc gcc gtg ggc gac gac aat atc cag caa cga 739 Ala Leu Leu Ala Ala Ser Ala Val Gly Asp Asp Asn Ile Gln Gln Arg 200 205 210 tcc ggt ggc gat gtc aat cct gaa agc tgg act cac ggc tca tcg cag 787 Ser Gly Gly Asp Val Asn Pro Glu Ser Trp Thr His Gly Ser Ser Gln 215 220 225 cag cgc aaa gac gcg ttc ctc gcc ggc tac aac acc ggc cag atg agc 835 Gln Arg Lys Asp Ala Phe Leu Ala Gly Tyr Asn Thr Gly Gln Met Ser 230 235 240 245 gcc tgc gac ttc ctc ggc cgg ggc gtc tac aac gac gct taaagcattg 884 Ala Cys Asp Phe Leu Gly Arg Gly Val Tyr Asn Asp Ala 250 255 cttttcgacg tct 897 16 258 PRT Corynebacterium glutamicum 16 Leu Leu Leu Gly Gly Asn Pro Ala Glu Ile Asp Gln Val Leu Gly Gly 1 5 10 15 Asp Gln Thr Gln Ile Glu Ser Gly Glu Ser Thr Gly Ala Gly Asp Phe 20 25 30 Asp His Cys Gln Thr Gly Ala Asp Ala Asn Ala Ser Asp Asp Cys Arg 35 40 45 Leu Tyr Tyr Thr Ser Phe Ser Val Asn Glu Met Trp Gln Thr Leu Leu 50 55 60 Pro Ala Gln Ala Gly Ile Glu Tyr Thr Glu Pro Thr Leu Thr Leu Phe 65 70 75 80 Lys Asn Ser Thr Gln Thr Gly Cys Gly Phe Ala Ser Ala Ser Thr Gly 85 90 95 Pro Phe Tyr Cys Pro Ser Asp Gln Asp Ala Tyr Phe Asp Leu Thr Phe 100 105 110 Phe Asp Gln Met Arg Gln Phe Gly Ala Glu Asn Ala Pro Leu Ala Gln 115 120 125 Met Tyr Ile Val Ala His Glu Tyr Gly His His Val Gln Asn Leu Glu 130 135 140 Gly Thr Leu Gly Leu Ser Asn Tyr Asn Asp Pro Gly Ala Asp Ser Asn 145 150 155 160 Ala Val Lys Ile Glu Leu Gln Ala Asp Cys Tyr Ala Gly Ile Trp Ala 165 170 175 Asn His Ser Ser Glu Gly Pro Asp Pro Leu Leu Gln Pro Ile Thr Glu 180 185 190 Ser Glu Leu Asp Ser Ala Leu Leu Ala Ala Ser Ala Val Gly Asp Asp 195 200 205 Asn Ile Gln Gln Arg Ser Gly Gly Asp Val Asn Pro Glu Ser Trp Thr 210 215 220 His Gly Ser Ser Gln Gln Arg Lys Asp Ala Phe Leu Ala Gly Tyr Asn 225 230 235 240 Thr Gly Gln Met Ser Ala Cys Asp Phe Leu Gly Arg Gly Val Tyr Asn 245 250 255 Asp Ala 17 771 DNA Corynebacterium glutamicum CDS (101)..(748) RXC01207 17 cttcatgatc tcaccggcag agcgcgtttt gttacagcgc gtaaactgtg actttgaaaa 60 atttttgaac aatccgtaca ccaacttcag gagaaaaaca gtg agc aga atc tat 115 Val Ser Arg Ile Tyr 1 5 gac tgt gcc gac caa gac tcc cgt gca gca ggc cta aag gcg gct gtc 163 Asp Cys Ala Asp Gln Asp Ser Arg Ala Ala Gly Leu Lys Ala Ala Val 10 15 20 gat gca gtc aaa gcc ggt cag ctc gtt gtc ctt ccc acg gat acc ctt 211 Asp Ala Val Lys Ala Gly Gln Leu Val Val Leu Pro Thr Asp Thr Leu 25 30 35 tat gga ctc ggc tgc gac gct ttc aac aac gag gca gta gcc aac ctt 259 Tyr Gly Leu Gly Cys Asp Ala Phe Asn Asn Glu Ala Val Ala Asn Leu 40 45 50 ctg gcc acc aaa cac cgt ggc ccc gat atg ccc gtt cca gtg ctc gtc 307 Leu Ala Thr Lys His Arg Gly Pro Asp Met Pro Val Pro Val Leu Val 55 60 65 ggc agc tgg gac acc att caa gga ctt gtg cac tcc tat tct gcg cag 355 Gly Ser Trp Asp Thr Ile Gln Gly Leu Val His Ser Tyr Ser Ala Gln 70 75 80 85 gca aaa gcg ctt gtg gag gcg ttc tgg cct ggt gga ctg tcc atc atc 403 Ala Lys Ala Leu Val Glu Ala Phe Trp Pro Gly Gly Leu Ser Ile Ile 90 95 100 gtt ccg cag gca cca agc ctt ccg tgg aac ctt ggc gat acc cgt ggc 451 Val Pro Gln Ala Pro Ser Leu Pro Trp Asn Leu Gly Asp Thr Arg Gly 105 110 115 acc gta atg ctg cgc atg cca ctg cac cca gtt gcc att gaa ttg ctg 499 Thr Val Met Leu Arg Met Pro Leu His Pro Val Ala Ile Glu Leu Leu 120 125 130 cgc caa acc gga cca atg gct gtc tcc tcc gcc aac atc tcc gga cat 547 Arg Gln Thr Gly Pro Met Ala Val Ser Ser Ala Asn Ile Ser Gly His 135 140 145 act cct cca acc acc gtg ctg gag gct cgt cag cag ctc aac caa aat 595 Thr Pro Pro Thr Thr Val Leu Glu Ala Arg Gln Gln Leu Asn Gln Asn 150 155 160 165 gtc gct gtc tac ctc gat ggt ggc gaa tgc gcg ctg gcc acc cct tca 643 Val Ala Val Tyr Leu Asp Gly Gly Glu Cys Ala Leu Ala Thr Pro Ser 170 175 180 acc atc gtg gat att tca ggc ccc gca cca aag att ttg cgt gag ggt 691 Thr Ile Val Asp Ile Ser Gly Pro Ala Pro Lys Ile Leu Arg Glu Gly 185 190 195 gcc atc agc gca gaa cgc gtt ggc gaa gta ctt gga gtg tcg gca gaa 739 Ala Ile Ser Ala Glu Arg Val Gly Glu Val Leu Gly Val Ser Ala Glu 200 205 210 agc ctg cgc taaatgggag tcggtttcgc ggg 771 Ser Leu Arg 215 18 216 PRT Corynebacterium glutamicum 18 Val Ser Arg Ile Tyr Asp Cys Ala Asp Gln Asp Ser Arg Ala Ala Gly 1 5 10 15 Leu Lys Ala Ala Val Asp Ala Val Lys Ala Gly Gln Leu Val Val Leu 20 25 30 Pro Thr Asp Thr Leu Tyr Gly Leu Gly Cys Asp Ala Phe Asn Asn Glu 35 40 45 Ala Val Ala Asn Leu Leu Ala Thr Lys His Arg Gly Pro Asp Met Pro 50 55 60 Val Pro Val Leu Val Gly Ser Trp Asp Thr Ile Gln Gly Leu Val His 65 70 75 80 Ser Tyr Ser Ala Gln Ala Lys Ala Leu Val Glu Ala Phe Trp Pro Gly 85 90 95 Gly Leu Ser Ile Ile Val Pro Gln Ala Pro Ser Leu Pro Trp Asn Leu 100 105 110 Gly Asp Thr Arg Gly Thr Val Met Leu Arg Met Pro Leu His Pro Val 115 120 125 Ala Ile Glu Leu Leu Arg Gln Thr Gly Pro Met Ala Val Ser Ser Ala 130 135 140 Asn Ile Ser Gly His Thr Pro Pro Thr Thr Val Leu Glu Ala Arg Gln 145 150 155 160 Gln Leu Asn Gln Asn Val Ala Val Tyr Leu Asp Gly Gly Glu Cys Ala 165 170 175 Leu Ala Thr Pro Ser Thr Ile Val Asp Ile Ser Gly Pro Ala Pro Lys 180 185 190 Ile Leu Arg Glu Gly Ala Ile Ser Ala Glu Arg Val Gly Glu Val Leu 195 200 205 Gly Val Ser Ala Glu Ser Leu Arg 210 215 19 1026 DNA Corynebacterium glutamicum CDS (101)..(1003) RXC00657 19 gtgcggatcg ggtatccgcg ctacacttag aggtgttaga gatcatgagt ttccacgaac 60 tgtaacgcag gattcaccaa tcaatgaaag gtcgaccgac atg agc act gaa gac 115 Met Ser Thr Glu Asp 1 5 att gtc gtc gta gca gta gat ggc tcg gac gcc tca aaa caa gct gtt 163 Ile Val Val Val Ala Val Asp Gly Ser Asp Ala Ser Lys Gln Ala Val 10 15 20 cgg tgg gct gca aat acc gcc aac aaa cgt ggc att cca ctt cgc ttg 211 Arg Trp Ala Ala Asn Thr Ala Asn Lys Arg Gly Ile Pro Leu Arg Leu 25 30 35 gct tcc agc tac acc atg cct cag ttc ctc tac gca gag gga atg gtt 259 Ala Ser Ser Tyr Thr Met Pro Gln Phe Leu Tyr Ala Glu Gly Met Val 40 45 50 cca cca caa gag ctt ttc gat gac ctc cag gcc gaa gcc ctg gaa aag 307 Pro Pro Gln Glu Leu Phe Asp Asp Leu Gln Ala Glu Ala Leu Glu Lys 55 60 65 att aac gaa gcc cgt gac atc gcc cat gag gta gcg cca gaa atc aag 355 Ile Asn Glu Ala Arg Asp Ile Ala His Glu Val Ala Pro Glu Ile Lys 70 75 80 85 atc ggg cac acc atc gct gaa ggc agt ccc atc gac atg ctg ttg gaa 403 Ile Gly His Thr Ile Ala Glu Gly Ser Pro Ile Asp Met Leu Leu Glu 90 95 100 atg tct ccc gat gcc aca atg atc gtc atg ggt tcc cgc gga ctc ggc 451 Met Ser Pro Asp Ala Thr Met Ile Val Met Gly Ser Arg Gly Leu Gly 105 110 115 gga ctc tcc gga atg gtc atg ggc tcc gtc tcc ggt gca gtg gtc agc 499 Gly Leu Ser Gly Met Val Met Gly Ser Val Ser Gly Ala Val Val Ser 120 125 130 cac gca aag tgt cca gtc gtt gtt gtc cgt gaa gac agc gca gtc aac 547 His Ala Lys Cys Pro Val Val Val Val Arg Glu Asp Ser Ala Val Asn 135 140 145 gaa gac agc aag tac ggc cca gtc gtc gtc ggt gtg gat ggc tcc gaa 595 Glu Asp Ser Lys Tyr Gly Pro Val Val Val Gly Val Asp Gly Ser Glu 150 155 160 165 gtc tcc caa cag gca acc gaa tac gca ttt gcg gaa gct gaa gct cgt 643 Val Ser Gln Gln Ala Thr Glu Tyr Ala Phe Ala Glu Ala Glu Ala Arg 170 175 180 ggc gcc gaa ctc gtt gca gtt cac acc tgg atg gac atg cag gta cag 691 Gly Ala Glu Leu Val Ala Val His Thr Trp Met Asp Met Gln Val Gln 185 190 195 gca tca ctt gca ggt ctt gca gct gct caa cag cag tgg gat gaa gtg 739 Ala Ser Leu Ala Gly Leu Ala Ala Ala Gln Gln Gln Trp Asp Glu Val 200 205 210 gaa cgt cag caa acc gac atg ctg atc gaa cgc ctc gca cca ctg gtg 787 Glu Arg Gln Gln Thr Asp Met Leu Ile Glu Arg Leu Ala Pro Leu Val 215 220 225 gaa aag tac cca agt gta acc gtc aag aag atc atc acc cgt gac cgc 835 Glu Lys Tyr Pro Ser Val Thr Val Lys Lys Ile Ile Thr Arg Asp Arg 230 235 240 245 cca gtt cgc gca ctt gca gaa gca tct gaa aac gcg cag ctc cta gtc 883 Pro Val Arg Ala Leu Ala Glu Ala Ser Glu Asn Ala Gln Leu Leu Val 250 255 260 gtt ggt tcc cat ggt cgt ggc gga ttt aag ggc atg ctc ctt ggc tcc 931 Val Gly Ser His Gly Arg Gly Gly Phe Lys Gly Met Leu Leu Gly Ser 265 270 275 acc tcc cgc gca ctg ctg caa tcc gca ccg tgc cca atg atg gtg gtt 979 Thr Ser Arg Ala Leu Leu Gln Ser Ala Pro Cys Pro Met Met Val Val 280 285 290 cgc cca cct gag aag att aag aag tagtttcttt taagtttcga tgc 1026 Arg Pro Pro Glu Lys Ile Lys Lys 295 300 20 301 PRT Corynebacterium glutamicum 20 Met Ser Thr Glu Asp Ile Val Val Val Ala Val Asp Gly Ser Asp Ala 1 5 10 15 Ser Lys Gln Ala Val Arg Trp Ala Ala Asn Thr Ala Asn Lys Arg Gly 20 25 30 Ile Pro Leu Arg Leu Ala Ser Ser Tyr Thr Met Pro Gln Phe Leu Tyr 35 40 45 Ala Glu Gly Met Val Pro Pro Gln Glu Leu Phe Asp Asp Leu Gln Ala 50 55 60 Glu Ala Leu Glu Lys Ile Asn Glu Ala Arg Asp Ile Ala His Glu Val 65 70 75 80 Ala Pro Glu Ile Lys Ile Gly His Thr Ile Ala Glu Gly Ser Pro Ile 85 90 95 Asp Met Leu Leu Glu Met Ser Pro Asp Ala Thr Met Ile Val Met Gly 100 105 110 Ser Arg Gly Leu Gly Gly Leu Ser Gly Met Val Met Gly Ser Val Ser 115 120 125 Gly Ala Val Val Ser His Ala Lys Cys Pro Val Val Val Val Arg Glu 130 135 140 Asp Ser Ala Val Asn Glu Asp Ser Lys Tyr Gly Pro Val Val Val Gly 145 150 155 160 Val Asp Gly Ser Glu Val Ser Gln Gln Ala Thr Glu Tyr Ala Phe Ala 165 170 175 Glu Ala Glu Ala Arg Gly Ala Glu Leu Val Ala Val His Thr Trp Met 180 185 190 Asp Met Gln Val Gln Ala Ser Leu Ala Gly Leu Ala Ala Ala Gln Gln 195 200 205 Gln Trp Asp Glu Val Glu Arg Gln Gln Thr Asp Met Leu Ile Glu Arg 210 215 220 Leu Ala Pro Leu Val Glu Lys Tyr Pro Ser Val Thr Val Lys Lys Ile 225 230 235 240 Ile Thr Arg Asp Arg Pro Val Arg Ala Leu Ala Glu Ala Ser Glu Asn 245 250 255 Ala Gln Leu Leu Val Val Gly Ser His Gly Arg Gly Gly Phe Lys Gly 260 265 270 Met Leu Leu Gly Ser Thr Ser Arg Ala Leu Leu Gln Ser Ala Pro Cys 275 280 285 Pro Met Met Val Val Arg Pro Pro Glu Lys Ile Lys Lys 290 295 300 21 1059 DNA Corynebacterium glutamicum CDS (101)..(1036) RXC00552 21 ccgccaacaa ggcagcaaag ctcgatccaa ttgacgcctt gcgttatgag taaaagcctc 60 gtttttaagg tagccacaca tcgcactaga ctgaagaact gtg gct acc tca aaa 115 Val Ala Thr Ser Lys 1 5 att ctt ctt tat tac gca ttc acc ccg ctc tct gac cct aaa gcg gtt 163 Ile Leu Leu Tyr Tyr Ala Phe Thr Pro Leu Ser Asp Pro Lys Ala Val 10 15 20 cag ctg tgg cag cgt gag ctc tgc gag tca ctg aat ctt cgt ggc cgc 211 Gln Leu Trp Gln Arg Glu Leu Cys Glu Ser Leu Asn Leu Arg Gly Arg 25 30 35 atc ctg atc tcc act cac ggc atc aat gga acc gtg ggc gga gat att 259 Ile Leu Ile Ser Thr His Gly Ile Asn Gly Thr Val Gly Gly Asp Ile 40 45 50 gat gat tgc aag gcg tac att aaa aag acc cgc gag tac cca ggt ttc 307 Asp Asp Cys Lys Ala Tyr Ile Lys Lys Thr Arg Glu Tyr Pro Gly Phe 55 60 65 aac cgc atg cag ttt aag tgg tcc gag ggt ggc gct gag gat ttc cca 355 Asn Arg Met Gln Phe Lys Trp Ser Glu Gly Gly Ala Glu Asp Phe Pro 70 75 80 85 aag ctc agt gtc aaa gtc cgc gat gag atc gtt gcc ttc ggc gct cca 403 Lys Leu Ser Val Lys Val Arg Asp Glu Ile Val Ala Phe Gly Ala Pro 90 95 100 gat gag ctc aaa gtg gat gaa aac ggc gtc gtc ggt ggc ggc gtt cac 451 Asp Glu Leu Lys Val Asp Glu Asn Gly Val Val Gly Gly Gly Val His 105 110 115 ctg aaa cca cag cag gtc aat gag ctt gtg gaa gcc cgt ggc gat gaa 499 Leu Lys Pro Gln Gln Val Asn Glu Leu Val Glu Ala Arg Gly Asp Glu 120 125 130 gtt gtg ttc ttt gac ggc cgc aac gca atg gaa gcc cag atc ggc aag 547 Val Val Phe Phe Asp Gly Arg Asn Ala Met Glu Ala Gln Ile Gly Lys 135 140 145 ttc aag gac gct gtt gtc cct gac gta gaa acc act cat gat ttc atc 595 Phe Lys Asp Ala Val Val Pro Asp Val Glu Thr Thr His Asp Phe Ile 150 155 160 165 gca gaa att gag tct gga aaa tac gac gat ctc aaa gac aag cct gtg 643 Ala Glu Ile Glu Ser Gly Lys Tyr Asp Asp Leu Lys Asp Lys Pro Val 170 175 180 gtc acc tac tgc acc ggc gga att cgt tgt gag atc ctg agt tca ctc 691 Val Thr Tyr Cys Thr Gly Gly Ile Arg Cys Glu Ile Leu Ser Ser Leu 185 190 195 atg atc aac cgt ggt ttc aaa gag gtc tac caa atc gat ggc ggc atc 739 Met Ile Asn Arg Gly Phe Lys Glu Val Tyr Gln Ile Asp Gly Gly Ile 200 205 210 gtt cgc tac ggc gag cag ttt ggc aac aag ggc ctg tgg gaa ggc tcc 787 Val Arg Tyr Gly Glu Gln Phe Gly Asn Lys Gly Leu Trp Glu Gly Ser 215 220 225 ctc tac gtt ttc gat aag cgc atg cat atg gaa ttc ggc gag gat tac 835 Leu Tyr Val Phe Asp Lys Arg Met His Met Glu Phe Gly Glu Asp Tyr 230 235 240 245 aaa gag gtc gga cac tgc atc cat tgc gat act ccc acc aac aaa ttt 883 Lys Glu Val Gly His Cys Ile His Cys Asp Thr Pro Thr Asn Lys Phe 250 255 260 gag cac tgc ctc aac gaa gat gat tgc cgc gag ctc gtg ttg atg tgc 931 Glu His Cys Leu Asn Glu Asp Asp Cys Arg Glu Leu Val Leu Met Cys 265 270 275 cct gat tgc ttc gcc aat gtt gag acc cgt cat tgc aag cgc gaa cgc 979 Pro Asp Cys Phe Ala Asn Val Glu Thr Arg His Cys Lys Arg Glu Arg 280 285 290 tgt gca gca att gct gcg gat ttc gct gag caa gga att gat ccg ctc 1027 Cys Ala Ala Ile Ala Ala Asp Phe Ala Glu Gln Gly Ile Asp Pro Leu 295 300 305 gtt act tct taaaaagggt atggtggctg ggt 1059 Val Thr Ser 310 22 312 PRT Corynebacterium glutamicum 22 Val Ala Thr Ser Lys Ile Leu Leu Tyr Tyr Ala Phe Thr Pro Leu Ser 1 5 10 15 Asp Pro Lys Ala Val Gln Leu Trp Gln Arg Glu Leu Cys Glu Ser Leu 20 25 30 Asn Leu Arg Gly Arg Ile Leu Ile Ser Thr His Gly Ile Asn Gly Thr 35 40 45 Val Gly Gly Asp Ile Asp Asp Cys Lys Ala Tyr Ile Lys Lys Thr Arg 50 55 60 Glu Tyr Pro Gly Phe Asn Arg Met Gln Phe Lys Trp Ser Glu Gly Gly 65 70 75 80 Ala Glu Asp Phe Pro Lys Leu Ser Val Lys Val Arg Asp Glu Ile Val 85 90 95 Ala Phe Gly Ala Pro Asp Glu Leu Lys Val Asp Glu Asn Gly Val Val 100 105 110 Gly Gly Gly Val His Leu Lys Pro Gln Gln Val Asn Glu Leu Val Glu 115 120 125 Ala Arg Gly Asp Glu Val Val Phe Phe Asp Gly Arg Asn Ala Met Glu 130 135 140 Ala Gln Ile Gly Lys Phe Lys Asp Ala Val Val Pro Asp Val Glu Thr 145 150 155 160 Thr His Asp Phe Ile Ala Glu Ile Glu Ser Gly Lys Tyr Asp Asp Leu 165 170 175 Lys Asp Lys Pro Val Val Thr Tyr Cys Thr Gly Gly Ile Arg Cys Glu 180 185 190 Ile Leu Ser Ser Leu Met Ile Asn Arg Gly Phe Lys Glu Val Tyr Gln 195 200 205 Ile Asp Gly Gly Ile Val Arg Tyr Gly Glu Gln Phe Gly Asn Lys Gly 210 215 220 Leu Trp Glu Gly Ser Leu Tyr Val Phe Asp Lys Arg Met His Met Glu 225 230 235 240 Phe Gly Glu Asp Tyr Lys Glu Val Gly His Cys Ile His Cys Asp Thr 245 250 255 Pro Thr Asn Lys Phe Glu His Cys Leu Asn Glu Asp Asp Cys Arg Glu 260 265 270 Leu Val Leu Met Cys Pro Asp Cys Phe Ala Asn Val Glu Thr Arg His 275 280 285 Cys Lys Arg Glu Arg Cys Ala Ala Ile Ala Ala Asp Phe Ala Glu Gln 290 295 300 Gly Ile Asp Pro Leu Val Thr Ser 305 310 23 1386 DNA Corynebacterium glutamicum CDS (101)..(1363) RXA00534 23 ctgtgcagaa agaaaacact cctctggcta ggtagacaca gtttataaag gtagagttga 60 gcgggtaact gtcagcacgt agatcgaaag gtgcacaaag gtg gcc ctg gtc gta 115 Val Ala Leu Val Val 1 5 cag aaa tat ggc ggt tcc tcg ctt gag agt gcg gaa cgc att aga aac 163 Gln Lys Tyr Gly Gly Ser Ser Leu Glu Ser Ala Glu Arg Ile Arg Asn 10 15 20 gtc gct gaa cgg atc gtt gcc acc aag aag gct gga aat gat gtc gtg 211 Val Ala Glu Arg Ile Val Ala Thr Lys Lys Ala Gly Asn Asp Val Val 25 30 35 gtt gtc tgc tcc gca atg gga gac acc acg gat gaa ctt cta gaa ctt 259 Val Val Cys Ser Ala Met Gly Asp Thr Thr Asp Glu Leu Leu Glu Leu 40 45 50 gca gcg gca gtg aat ccc gtt ccg cca gct cgt gaa atg gat atg ctc 307 Ala Ala Ala Val Asn Pro Val Pro Pro Ala Arg Glu Met Asp Met Leu 55 60 65 ctg act gct ggt gag cgt att tct aac gct ctc gtc gcc atg gct att 355 Leu Thr Ala Gly Glu Arg Ile Ser Asn Ala Leu Val Ala Met Ala Ile 70 75 80 85 gag tcc ctt ggc gca gaa gcc caa tct ttc acg ggc tct cag gct ggt 403 Glu Ser Leu Gly Ala Glu Ala Gln Ser Phe Thr Gly Ser Gln Ala Gly 90 95 100 gtg ctc acc acc gag cgc cac gga aac gca cgc att gtt gat gtc act 451 Val Leu Thr Thr Glu Arg His Gly Asn Ala Arg Ile Val Asp Val Thr 105 110 115 cca ggt cgt gtg cgt gaa gca ctc gat gag ggc aag atc tgc att gtt 499 Pro Gly Arg Val Arg Glu Ala Leu Asp Glu Gly Lys Ile Cys Ile Val 120 125 130 gct ggt ttc cag ggt gtt aat aaa gaa acc cgc gat gtc acc acg ttg 547 Ala Gly Phe Gln Gly Val Asn Lys Glu Thr Arg Asp Val Thr Thr Leu 135 140 145 ggt cgt ggt ggt tct gac acc act gca gtt gcg ttg gca gct gct ttg 595 Gly Arg Gly Gly Ser Asp Thr Thr Ala Val Ala Leu Ala Ala Ala Leu 150 155 160 165 aac gct gat gtg tgt gag att tac tcg gac gtt gac ggt gtg tat acc 643 Asn Ala Asp Val Cys Glu Ile Tyr Ser Asp Val Asp Gly Val Tyr Thr 170 175 180 gct gac ccg cgc atc gtt cct aat gca cag aag ctg gaa aag ctc agc 691 Ala Asp Pro Arg Ile Val Pro Asn Ala Gln Lys Leu Glu Lys Leu Ser 185 190 195 ttc gaa gaa atg ctg gaa ctt gct gct gtt ggc tcc aag att ttg gtg 739 Phe Glu Glu Met Leu Glu Leu Ala Ala Val Gly Ser Lys Ile Leu Val 200 205 210 ctg cgc agt gtt gaa tac gct cgt gca ttc aat gtg cca ctt cgc gta 787 Leu Arg Ser Val Glu Tyr Ala Arg Ala Phe Asn Val Pro Leu Arg Val 215 220 225 cgc tcg tct tat agt aat gat ccc ggc act ttg att gcc ggc tct atg 835 Arg Ser Ser Tyr Ser Asn Asp Pro Gly Thr Leu Ile Ala Gly Ser Met 230 235 240 245 gag gat att cct gtg gaa gaa gca gtc ctt acc ggt gtc gca acc gac 883 Glu Asp Ile Pro Val Glu Glu Ala Val Leu Thr Gly Val Ala Thr Asp 250 255 260 aag tcc gaa gcc aaa gta acc gtt ctg ggt att tcc gat aag cca ggc 931 Lys Ser Glu Ala Lys Val Thr Val Leu Gly Ile Ser Asp Lys Pro Gly 265 270 275 gag gct gcg aag gtt ttc cgt gcg ttg gct gat gca gaa atc aac att 979 Glu Ala Ala Lys Val Phe Arg Ala Leu Ala Asp Ala Glu Ile Asn Ile 280 285 290 gac atg gtt ctg cag aac gtc tct tct gta gaa gac ggc acc acc gac 1027 Asp Met Val Leu Gln Asn Val Ser Ser Val Glu Asp Gly Thr Thr Asp 295 300 305 atc acc ttc acc tgc cct cgt tcc gac ggc cgc cgc gcg atg gag atc 1075 Ile Thr Phe Thr Cys Pro Arg Ser Asp Gly Arg Arg Ala Met Glu Ile 310 315 320 325 ttg aag aag ctt cag gtt cag ggc aac tgg acc aat gtg ctt tac gac 1123 Leu Lys Lys Leu Gln Val Gln Gly Asn Trp Thr Asn Val Leu Tyr Asp 330 335 340 gac cag gtc ggc aaa gtc tcc ctc gtg ggt gct ggc atg aag tct cac 1171 Asp Gln Val Gly Lys Val Ser Leu Val Gly Ala Gly Met Lys Ser His 345 350 355 cca ggt gtt acc gca gag ttc atg gaa gct ctg cgc gat gtc aac gtg 1219 Pro Gly Val Thr Ala Glu Phe Met Glu Ala Leu Arg Asp Val Asn Val 360 365 370 aac atc gaa ttg att tcc acc tct gag att cgt att tcc gtg ctg atc 1267 Asn Ile Glu Leu Ile Ser Thr Ser Glu Ile Arg Ile Ser Val Leu Ile 375 380 385 cgt gaa gat gat ctg gat gct gct gca cgt gca ttg cat gag cag ttc 1315 Arg Glu Asp Asp Leu Asp Ala Ala Ala Arg Ala Leu His Glu Gln Phe 390 395 400 405 cag ctg ggc ggc gaa gac gaa gcc gtc gtt tat gca ggc acc gga cgc 1363 Gln Leu Gly Gly Glu Asp Glu Ala Val Val Tyr Ala Gly Thr Gly Arg 410 415 420 taaagtttta aaggagtagt ttt 1386 24 421 PRT Corynebacterium glutamicum 24 Val Ala Leu Val Val Gln Lys Tyr Gly Gly Ser Ser Leu Glu Ser Ala 1 5 10 15 Glu Arg Ile Arg Asn Val Ala Glu Arg Ile Val Ala Thr Lys Lys Ala 20 25 30 Gly Asn Asp Val Val Val Val Cys Ser Ala Met Gly Asp Thr Thr Asp 35 40 45 Glu Leu Leu Glu Leu Ala Ala Ala Val Asn Pro Val Pro Pro Ala Arg 50 55 60 Glu Met Asp Met Leu Leu Thr Ala Gly Glu Arg Ile Ser Asn Ala Leu 65 70 75 80 Val Ala Met Ala Ile Glu Ser Leu Gly Ala Glu Ala Gln Ser Phe Thr 85 90 95 Gly Ser Gln Ala Gly Val Leu Thr Thr Glu Arg His Gly Asn Ala Arg 100 105 110 Ile Val Asp Val Thr Pro Gly Arg Val Arg Glu Ala Leu Asp Glu Gly 115 120 125 Lys Ile Cys Ile Val Ala Gly Phe Gln Gly Val Asn Lys Glu Thr Arg 130 135 140 Asp Val Thr Thr Leu Gly Arg Gly Gly Ser Asp Thr Thr Ala Val Ala 145 150 155 160 Leu Ala Ala Ala Leu Asn Ala Asp Val Cys Glu Ile Tyr Ser Asp Val 165 170 175 Asp Gly Val Tyr Thr Ala Asp Pro Arg Ile Val Pro Asn Ala Gln Lys 180 185 190 Leu Glu Lys Leu Ser Phe Glu Glu Met Leu Glu Leu Ala Ala Val Gly 195 200 205 Ser Lys Ile Leu Val Leu Arg Ser Val Glu Tyr Ala Arg Ala Phe Asn 210 215 220 Val Pro Leu Arg Val Arg Ser Ser Tyr Ser Asn Asp Pro Gly Thr Leu 225 230 235 240 Ile Ala Gly Ser Met Glu Asp Ile Pro Val Glu Glu Ala Val Leu Thr 245 250 255 Gly Val Ala Thr Asp Lys Ser Glu Ala Lys Val Thr Val Leu Gly Ile 260 265 270 Ser Asp Lys Pro Gly Glu Ala Ala Lys Val Phe Arg Ala Leu Ala Asp 275 280 285 Ala Glu Ile Asn Ile Asp Met Val Leu Gln Asn Val Ser Ser Val Glu 290 295 300 Asp Gly Thr Thr Asp Ile Thr Phe Thr Cys Pro Arg Ser Asp Gly Arg 305 310 315 320 Arg Ala Met Glu Ile Leu Lys Lys Leu Gln Val Gln Gly Asn Trp Thr 325 330 335 Asn Val Leu Tyr Asp Asp Gln Val Gly Lys Val Ser Leu Val Gly Ala 340 345 350 Gly Met Lys Ser His Pro Gly Val Thr Ala Glu Phe Met Glu Ala Leu 355 360 365 Arg Asp Val Asn Val Asn Ile Glu Leu Ile Ser Thr Ser Glu Ile Arg 370 375 380 Ile Ser Val Leu Ile Arg Glu Asp Asp Leu Asp Ala Ala Ala Arg Ala 385 390 395 400 Leu His Glu Gln Phe Gln Leu Gly Gly Glu Asp Glu Ala Val Val Tyr 405 410 415 Ala Gly Thr Gly Arg 420 25 1155 DNA Corynebacterium glutamicum CDS (101)..(1132) RXA00533 25 ctgcacgtgc attgcatgag cagttccagc tgggcggcga agacgaagcc gtcgtttatg 60 caggcaccgg acgctaaagt tttaaaggag tagttttaca atg acc acc atc gca 115 Met Thr Thr Ile Ala 1 5 gtt gtt ggt gca acc ggc cag gtc ggc cag gtt atg cgc acc ctt ttg 163 Val Val Gly Ala Thr Gly Gln Val Gly Gln Val Met Arg Thr Leu Leu 10 15 20 gaa gag cgc aat ttc cca gct gac act gtt cgt ttc ttt gct tcc cca 211 Glu Glu Arg Asn Phe Pro Ala Asp Thr Val Arg Phe Phe Ala Ser Pro 25 30 35 cgt tcc gca ggc cgt aag att gaa ttc cgt ggc acg gaa atc gag gta 259 Arg Ser Ala Gly Arg Lys Ile Glu Phe Arg Gly Thr Glu Ile Glu Val 40 45 50 gaa gac att act cag gca acc gag gag tcc ctc aag gac atc gac gtt 307 Glu Asp Ile Thr Gln Ala Thr Glu Glu Ser Leu Lys Asp Ile Asp Val 55 60 65 gcg ttg ttc tcc gct gga ggc acc gct tcc aag cag tac gct cca ctg 355 Ala Leu Phe Ser Ala Gly Gly Thr Ala Ser Lys Gln Tyr Ala Pro Leu 70 75 80 85 ttc gct gct gca ggc gcg act gtt gtg gat aac tct tct gct tgg cgc 403 Phe Ala Ala Ala Gly Ala Thr Val Val Asp Asn Ser Ser Ala Trp Arg 90 95 100 aag gac gac gag gtt cca cta atc gtc tct gag gtg aac cct tcc gac 451 Lys Asp Asp Glu Val Pro Leu Ile Val Ser Glu Val Asn Pro Ser Asp 105 110 115 aag gat tcc ctg gtc aag ggc att att gcg aac cct aac tgc acc acc 499 Lys Asp Ser Leu Val Lys Gly Ile Ile Ala Asn Pro Asn Cys Thr Thr 120 125 130 atg gct gcg atg cca gtg ctg aag cca ctt cac gat gcc gct ggt ctt 547 Met Ala Ala Met Pro Val Leu Lys Pro Leu His Asp Ala Ala Gly Leu 135 140 145 gta aag ctt cac gtt tcc tct tac cag gct gtt tcc ggt tct ggt ctt 595 Val Lys Leu His Val Ser Ser Tyr Gln Ala Val Ser Gly Ser Gly Leu 150 155 160 165 gca ggt gtg gaa acc ttg gca aag cag gtt gct gca gtt gga gac cac 643 Ala Gly Val Glu Thr Leu Ala Lys Gln Val Ala Ala Val Gly Asp His 170 175 180 aac gtt gag ttc gtc cat gat gga cag gct gct gac gca ggc gat gtc 691 Asn Val Glu Phe Val His Asp Gly Gln Ala Ala Asp Ala Gly Asp Val 185 190 195 gga cct tat gtt tca cca atc gct tac aac gtg ctg cca ttc gcc gga 739 Gly Pro Tyr Val Ser Pro Ile Ala Tyr Asn Val Leu Pro Phe Ala Gly 200 205 210 aac ctc gtc gat gac ggc acc ttc gaa acc gat gaa gag cag aag ctg 787 Asn Leu Val Asp Asp Gly Thr Phe Glu Thr Asp Glu Glu Gln Lys Leu 215 220 225 cgc aac gaa tcc cgc aag att ctc ggt ctc cca gac ctc aag gtc tca 835 Arg Asn Glu Ser Arg Lys Ile Leu Gly Leu Pro Asp Leu Lys Val Ser 230 235 240 245 ggc acc tgc gtc cgc gtg ccg gtt ttc acc ggc cac acg ctg acc att 883 Gly Thr Cys Val Arg Val Pro Val Phe Thr Gly His Thr Leu Thr Ile 250 255 260 cac gcc gaa ttc gac aag gca atc acc gtg gac cag gcg cag gag atc 931 His Ala Glu Phe Asp Lys Ala Ile Thr Val Asp Gln Ala Gln Glu Ile 265 270 275 ttg ggt gcc gct tca ggc gtc aag ctt gtc gac gtc cca acc cca ctt 979 Leu Gly Ala Ala Ser Gly Val Lys Leu Val Asp Val Pro Thr Pro Leu 280 285 290 gca gct gcc ggc att gac gaa tcc ctc gtt gga cgc atc cgt cag gac 1027 Ala Ala Ala Gly Ile Asp Glu Ser Leu Val Gly Arg Ile Arg Gln Asp 295 300 305 tcc act gtc gac gat aac cgc ggt ctg gtt ctc gtc gta tct ggc gac 1075 Ser Thr Val Asp Asp Asn Arg Gly Leu Val Leu Val Val Ser Gly Asp 310 315 320 325 aac ctc cgc aag ggt gct gcg cta aac acc atc cag atc gct gag ctg 1123 Asn Leu Arg Lys Gly Ala Ala Leu Asn Thr Ile Gln Ile Ala Glu Leu 330 335 340 ctg gtt aag taaaaacccg ccattaaaaa ctc 1155 Leu Val Lys 26 344 PRT Corynebacterium glutamicum 26 Met Thr Thr Ile Ala Val Val Gly Ala Thr Gly Gln Val Gly Gln Val 1 5 10 15 Met Arg Thr Leu Leu Glu Glu Arg Asn Phe Pro Ala Asp Thr Val Arg 20 25 30 Phe Phe Ala Ser Pro Arg Ser Ala Gly Arg Lys Ile Glu Phe Arg Gly 35 40 45 Thr Glu Ile Glu Val Glu Asp Ile Thr Gln Ala Thr Glu Glu Ser Leu 50 55 60 Lys Asp Ile Asp Val Ala Leu Phe Ser Ala Gly Gly Thr Ala Ser Lys 65 70 75 80 Gln Tyr Ala Pro Leu Phe Ala Ala Ala Gly Ala Thr Val Val Asp Asn 85 90 95 Ser Ser Ala Trp Arg Lys Asp Asp Glu Val Pro Leu Ile Val Ser Glu 100 105 110 Val Asn Pro Ser Asp Lys Asp Ser Leu Val Lys Gly Ile Ile Ala Asn 115 120 125 Pro Asn Cys Thr Thr Met Ala Ala Met Pro Val Leu Lys Pro Leu His 130 135 140 Asp Ala Ala Gly Leu Val Lys Leu His Val Ser Ser Tyr Gln Ala Val 145 150 155 160 Ser Gly Ser Gly Leu Ala Gly Val Glu Thr Leu Ala Lys Gln Val Ala 165 170 175 Ala Val Gly Asp His Asn Val Glu Phe Val His Asp Gly Gln Ala Ala 180 185 190 Asp Ala Gly Asp Val Gly Pro Tyr Val Ser Pro Ile Ala Tyr Asn Val 195 200 205 Leu Pro Phe Ala Gly Asn Leu Val Asp Asp Gly Thr Phe Glu Thr Asp 210 215 220 Glu Glu Gln Lys Leu Arg Asn Glu Ser Arg Lys Ile Leu Gly Leu Pro 225 230 235 240 Asp Leu Lys Val Ser Gly Thr Cys Val Arg Val Pro Val Phe Thr Gly 245 250 255 His Thr Leu Thr Ile His Ala Glu Phe Asp Lys Ala Ile Thr Val Asp 260 265 270 Gln Ala Gln Glu Ile Leu Gly Ala Ala Ser Gly Val Lys Leu Val Asp 275 280 285 Val Pro Thr Pro Leu Ala Ala Ala Gly Ile Asp Glu Ser Leu Val Gly 290 295 300 Arg Ile Arg Gln Asp Ser Thr Val Asp Asp Asn Arg Gly Leu Val Leu 305 310 315 320 Val Val Ser Gly Asp Asn Leu Arg Lys Gly Ala Ala Leu Asn Thr Ile 325 330 335 Gln Ile Ala Glu Leu Leu Val Lys 340 27 608 DNA Corynebacterium glutamicum CDS (69)..(608) RXA02843 27 cccattgcgc ggaggtcgca ccccttccga cttgaactga taggccgata gaaattattc 60 tggacgtc atg act act gct tcc gca acc gga att gca aca ctg acc tcc 110 Met Thr Thr Ala Ser Ala Thr Gly Ile Ala Thr Leu Thr Ser 1 5 10 acc ggc gac gtc ctg gac gtg tgg tat cca gaa atc ggg tcc acc gac 158 Thr Gly Asp Val Leu Asp Val Trp Tyr Pro Glu Ile Gly Ser Thr Asp 15 20 25 30 cag tcc gcg ctc aca cct cta gaa ggc gtc gat gaa gat cga aac gtc 206 Gln Ser Ala Leu Thr Pro Leu Glu Gly Val Asp Glu Asp Arg Asn Val 35 40 45 acc cgc aaa atc gtg acg aca act atc gac acc gac gca gcc ccc acc 254 Thr Arg Lys Ile Val Thr Thr Thr Ile Asp Thr Asp Ala Ala Pro Thr 50 55 60 gac acc tac gat gca tgg ctg cgc ctt cac ctc ctc tcc cac cgc gtt 302 Asp Thr Tyr Asp Ala Trp Leu Arg Leu His Leu Leu Ser His Arg Val 65 70 75 ttc cgc cct cac acc atc aac cta gac ggc att ttc ggc ctc ctc aac 350 Phe Arg Pro His Thr Ile Asn Leu Asp Gly Ile Phe Gly Leu Leu Asn 80 85 90 aat gtc gtg tgg acc aac ttc gga ccg tgc gca gtt gac ggt ttc gca 398 Asn Val Val Trp Thr Asn Phe Gly Pro Cys Ala Val Asp Gly Phe Ala 95 100 105 110 ctc acc cgc gcg cgc ctg tca cgc cga ggc caa gtt acg gtt tat agc 446 Leu Thr Arg Ala Arg Leu Ser Arg Arg Gly Gln Val Thr Val Tyr Ser 115 120 125 gtc gac aag ttc cca cgc atg gtc gac tat gtg gtt ccc tcg ggc gtg 494 Val Asp Lys Phe Pro Arg Met Val Asp Tyr Val Val Pro Ser Gly Val 130 135 140 cgc atc ggt gac gcc gac cgc gtc cga ctt ggc gcg tac ctg gca gat 542 Arg Ile Gly Asp Ala Asp Arg Val Arg Leu Gly Ala Tyr Leu Ala Asp 145 150 155 ggc acc acc gtg atg cat gag ggc ttc gtg aac ttc aac gct ggc acg 590 Gly Thr Thr Val Met His Glu Gly Phe Val Asn Phe Asn Ala Gly Thr 160 165 170 ctc ggc gct tcc atg gtt 608 Leu Gly Ala Ser Met Val 175 180 28 180 PRT Corynebacterium glutamicum 28 Met Thr Thr Ala Ser Ala Thr Gly Ile Ala Thr Leu Thr Ser Thr Gly 1 5 10 15 Asp Val Leu Asp Val Trp Tyr Pro Glu Ile Gly Ser Thr Asp Gln Ser 20 25 30 Ala Leu Thr Pro Leu Glu Gly Val Asp Glu Asp Arg Asn Val Thr Arg 35 40 45 Lys Ile Val Thr Thr Thr Ile Asp Thr Asp Ala Ala Pro Thr Asp Thr 50 55 60 Tyr Asp Ala Trp Leu Arg Leu His Leu Leu Ser His Arg Val Phe Arg 65 70 75 80 Pro His Thr Ile Asn Leu Asp Gly Ile Phe Gly Leu Leu Asn Asn Val 85 90 95 Val Trp Thr Asn Phe Gly Pro Cys Ala Val Asp Gly Phe Ala Leu Thr 100 105 110 Arg Ala Arg Leu Ser Arg Arg Gly Gln Val Thr Val Tyr Ser Val Asp 115 120 125 Lys Phe Pro Arg Met Val Asp Tyr Val Val Pro Ser Gly Val Arg Ile 130 135 140 Gly Asp Ala Asp Arg Val Arg Leu Gly Ala Tyr Leu Ala Asp Gly Thr 145 150 155 160 Thr Val Met His Glu Gly Phe Val Asn Phe Asn Ala Gly Thr Leu Gly 165 170 175 Ala Ser Met Val 180 29 1230 DNA Corynebacterium glutamicum CDS (101)..(1207) RXA02022 29 tatttgcgat tccaactgct tgggctccgc gaatgttttc actcattttt taatcgaccg 60 cttccatcat gttttaacta aggtttgtag gcttaaacct gtg aac tct gaa ctc 115 Val Asn Ser Glu Leu 1 5 aaa cca gga tta gat ctc ctc ggc gac cca att gtc ctt act caa cgt 163 Lys Pro Gly Leu Asp Leu Leu Gly Asp Pro Ile Val Leu Thr Gln Arg 10 15 20 ttg gta gat ata ccg agt ccg tcg ggt cag gaa aag cag att gct gat 211 Leu Val Asp Ile Pro Ser Pro Ser Gly Gln Glu Lys Gln Ile Ala Asp 25 30 35 gaa att gaa gat gcc ctt cgg aac ctt aat cta cct ggt gta gag gtc 259 Glu Ile Glu Asp Ala Leu Arg Asn Leu Asn Leu Pro Gly Val Glu Val 40 45 50 ttc cgc ttc aac aac aac gtt ctt gct cgc acg aac agg gga ttg gcc 307 Phe Arg Phe Asn Asn Asn Val Leu Ala Arg Thr Asn Arg Gly Leu Ala 55 60 65 tcg agg gtc atg ctt gct ggt cat atc gat aca gtg ccg atc gcg gac 355 Ser Arg Val Met Leu Ala Gly His Ile Asp Thr Val Pro Ile Ala Asp 70 75 80 85 aat ctg cca agc cgt gtg gaa gac ggc atc atg tat ggc tgt ggc acc 403 Asn Leu Pro Ser Arg Val Glu Asp Gly Ile Met Tyr Gly Cys Gly Thr 90 95 100 gtc gat atg aaa tct ggg ttg gcg gtg tat ttg cat act ttt gcc acc 451 Val Asp Met Lys Ser Gly Leu Ala Val Tyr Leu His Thr Phe Ala Thr 105 110 115 ttg gcc acg tcg act gag ctt aaa cat gat ctg acg ctg att gcg tat 499 Leu Ala Thr Ser Thr Glu Leu Lys His Asp Leu Thr Leu Ile Ala Tyr 120 125 130 gag tgc gag gaa gtt gct gat cac ctc aat ggt ttg ggc cac att cgc 547 Glu Cys Glu Glu Val Ala Asp His Leu Asn Gly Leu Gly His Ile Arg 135 140 145 gat gag cat ccg gag tgg ttg gcg gct gat ttg gcg ttg ttg ggt gag 595 Asp Glu His Pro Glu Trp Leu Ala Ala Asp Leu Ala Leu Leu Gly Glu 150 155 160 165 cct act ggc ggc tgg att gag gcg ggc tgc cag ggc aat ctg cgc atc 643 Pro Thr Gly Gly Trp Ile Glu Ala Gly Cys Gln Gly Asn Leu Arg Ile 170 175 180 aag gtg acg gcg cat ggt gtg cgt gcc cat tcg gcg aga agc tgg ttg 691 Lys Val Thr Ala His Gly Val Arg Ala His Ser Ala Arg Ser Trp Leu 185 190 195 ggt gat aat gcg atg cat aag ttg tcg ccg atc att tcg aag gtt gct 739 Gly Asp Asn Ala Met His Lys Leu Ser Pro Ile Ile Ser Lys Val Ala 200 205 210 gcg tat aag gcc gca gaa gtc aac att gat ggc ttg acc tac cgt gaa 787 Ala Tyr Lys Ala Ala Glu Val Asn Ile Asp Gly Leu Thr Tyr Arg Glu 215 220 225 ggc ctc aac atc gtt ttc tgc gaa tcg ggc gtg gca aac aac gtc att 835 Gly Leu Asn Ile Val Phe Cys Glu Ser Gly Val Ala Asn Asn Val Ile 230 235 240 245 cca gac ctc gcg tgg atg aac ctc aac ttc cgt ttc gcg ccg aat cgc 883 Pro Asp Leu Ala Trp Met Asn Leu Asn Phe Arg Phe Ala Pro Asn Arg 250 255 260 gat ctc aac gag gcg atc gag cat gtc gtc gaa acg ctt gag ctt gac 931 Asp Leu Asn Glu Ala Ile Glu His Val Val Glu Thr Leu Glu Leu Asp 265 270 275 ggt caa gac ggc atc gaa tgg gcc gta gaa gac ggg gca ggc ggt gcc 979 Gly Gln Asp Gly Ile Glu Trp Ala Val Glu Asp Gly Ala Gly Gly Ala 280 285 290 ctt cca ggc ttg ggg cag cag gtg aca agc ggg ctt atc gac gcc gtc 1027 Leu Pro Gly Leu Gly Gln Gln Val Thr Ser Gly Leu Ile Asp Ala Val 295 300 305 ggc cgc gaa aaa atc cgc gca aaa ttc ggc tgg acc gat gtc tca cgt 1075 Gly Arg Glu Lys Ile Arg Ala Lys Phe Gly Trp Thr Asp Val Ser Arg 310 315 320 325 ttt tca gcc atg gga att cca gcc cta aac ttt ggc gct ggt gat cca 1123 Phe Ser Ala Met Gly Ile Pro Ala Leu Asn Phe Gly Ala Gly Asp Pro 330 335 340 agt ttc gcg cat aaa cgc gac gag cag tgc cca gtg gag caa atc acg 1171 Ser Phe Ala His Lys Arg Asp Glu Gln Cys Pro Val Glu Gln Ile Thr 345 350 355 gat gtg gca gca att ttg aag cag tac ctg agc gag taaccgcatt 1217 Asp Val Ala Ala Ile Leu Lys Gln Tyr Leu Ser Glu 360 365 cggggttatc gtg 1230 30 369 PRT Corynebacterium glutamicum 30 Val Asn Ser Glu Leu Lys Pro Gly Leu Asp Leu Leu Gly Asp Pro Ile 1 5 10 15 Val Leu Thr Gln Arg Leu Val Asp Ile Pro Ser Pro Ser Gly Gln Glu 20 25 30 Lys Gln Ile Ala Asp Glu Ile Glu Asp Ala Leu Arg Asn Leu Asn Leu 35 40 45 Pro Gly Val Glu Val Phe Arg Phe Asn Asn Asn Val Leu Ala Arg Thr 50 55 60 Asn Arg Gly Leu Ala Ser Arg Val Met Leu Ala Gly His Ile Asp Thr 65 70 75 80 Val Pro Ile Ala Asp Asn Leu Pro Ser Arg Val Glu Asp Gly Ile Met 85 90 95 Tyr Gly Cys Gly Thr Val Asp Met Lys Ser Gly Leu Ala Val Tyr Leu 100 105 110 His Thr Phe Ala Thr Leu Ala Thr Ser Thr Glu Leu Lys His Asp Leu 115 120 125 Thr Leu Ile Ala Tyr Glu Cys Glu Glu Val Ala Asp His Leu Asn Gly 130 135 140 Leu Gly His Ile Arg Asp Glu His Pro Glu Trp Leu Ala Ala Asp Leu 145 150 155 160 Ala Leu Leu Gly Glu Pro Thr Gly Gly Trp Ile Glu Ala Gly Cys Gln 165 170 175 Gly Asn Leu Arg Ile Lys Val Thr Ala His Gly Val Arg Ala His Ser 180 185 190 Ala Arg Ser Trp Leu Gly Asp Asn Ala Met His Lys Leu Ser Pro Ile 195 200 205 Ile Ser Lys Val Ala Ala Tyr Lys Ala Ala Glu Val Asn Ile Asp Gly 210 215 220 Leu Thr Tyr Arg Glu Gly Leu Asn Ile Val Phe Cys Glu Ser Gly Val 225 230 235 240 Ala Asn Asn Val Ile Pro Asp Leu Ala Trp Met Asn Leu Asn Phe Arg 245 250 255 Phe Ala Pro Asn Arg Asp Leu Asn Glu Ala Ile Glu His Val Val Glu 260 265 270 Thr Leu Glu Leu Asp Gly Gln Asp Gly Ile Glu Trp Ala Val Glu Asp 275 280 285 Gly Ala Gly Gly Ala Leu Pro Gly Leu Gly Gln Gln Val Thr Ser Gly 290 295 300 Leu Ile Asp Ala Val Gly Arg Glu Lys Ile Arg Ala Lys Phe Gly Trp 305 310 315 320 Thr Asp Val Ser Arg Phe Ser Ala Met Gly Ile Pro Ala Leu Asn Phe 325 330 335 Gly Ala Gly Asp Pro Ser Phe Ala His Lys Arg Asp Glu Gln Cys Pro 340 345 350 Val Glu Gln Ile Thr Asp Val Ala Ala Ile Leu Lys Gln Tyr Leu Ser 355 360 365 Glu 31 1059 DNA Corynebacterium glutamicum CDS (101)..(1036) RXA00044 31 attacctcag ccttccaagc tgatgatgca ttacttaaaa actgcagaca cttgaaaaac 60 ttctcacccg cactcgttcc ctcaacccac aaggagcacc atg gct tcc gca act 115 Met Ala Ser Ala Thr 1 5 ttc acc ggc gtg atc cca ccc gta atg acc cca ctc cac gcc gac ggc 163 Phe Thr Gly Val Ile Pro Pro Val Met Thr Pro Leu His Ala Asp Gly 10 15 20 agt gtg gat gta gaa agc ctc cgc aag ctc gtt gac cac ctc atc aat 211 Ser Val Asp Val Glu Ser Leu Arg Lys Leu Val Asp His Leu Ile Asn 25 30 35 ggt ggc gtc gac gga ctt ttc gca ctg ggc tcc tca ggc gaa gcg gca 259 Gly Gly Val Asp Gly Leu Phe Ala Leu Gly Ser Ser Gly Glu Ala Ala 40 45 50 ttc ctc acc cgc gcc cag cgc aaa ctc gca ctg acc acc atc atc gag 307 Phe Leu Thr Arg Ala Gln Arg Lys Leu Ala Leu Thr Thr Ile Ile Glu 55 60 65 cac acc gca ggc cgc gtt ccc gta act gct ggt gtc att gaa acc acc 355 His Thr Ala Gly Arg Val Pro Val Thr Ala Gly Val Ile Glu Thr Thr 70 75 80 85 act gct cgc gtg att gag ctc gtg gaa gat gcc ctg gag gct ggt gcc 403 Thr Ala Arg Val Ile Glu Leu Val Glu Asp Ala Leu Glu Ala Gly Ala 90 95 100 gaa ggc ctc gtt gcc act gca cct ttc tac acc cgc acc cac gat gtg 451 Glu Gly Leu Val Ala Thr Ala Pro Phe Tyr Thr Arg Thr His Asp Val 105 110 115 gaa att gaa gaa cac ttc cgc aag atc cac gcc gcc gct cca gag ctt 499 Glu Ile Glu Glu His Phe Arg Lys Ile His Ala Ala Ala Pro Glu Leu 120 125 130 cca ctg ttt gcc tac aac atc cca gtg tcg gtg cac tcc aac ctc aac 547 Pro Leu Phe Ala Tyr Asn Ile Pro Val Ser Val His Ser Asn Leu Asn 135 140 145 cca gtc atg ctt ttg acg ctg gcc aag gat ggc gtt ctt gca ggc acc 595 Pro Val Met Leu Leu Thr Leu Ala Lys Asp Gly Val Leu Ala Gly Thr 150 155 160 165 aag gat tcc agt ggc aat gat ggc gca atc cgc tca ctg atc gaa gct 643 Lys Asp Ser Ser Gly Asn Asp Gly Ala Ile Arg Ser Leu Ile Glu Ala 170 175 180 cgt gat gat gct gga ctc act gag cag ttc aag atc ctc acc ggc agc 691 Arg Asp Asp Ala Gly Leu Thr Glu Gln Phe Lys Ile Leu Thr Gly Ser 185 190 195 gaa acc acc gtt gat ttc gcc tac ctt gcg ggt gcc gat gga gtt gtc 739 Glu Thr Thr Val Asp Phe Ala Tyr Leu Ala Gly Ala Asp Gly Val Val 200 205 210 cca ggc ctg ggc aat gtt gat cct gca gca tac gca gct tta gca aaa 787 Pro Gly Leu Gly Asn Val Asp Pro Ala Ala Tyr Ala Ala Leu Ala Lys 215 220 225 ctc tgc ctc gat gga aag tgg gca gaa gct gct gct ttg cag aag cgc 835 Leu Cys Leu Asp Gly Lys Trp Ala Glu Ala Ala Ala Leu Gln Lys Arg 230 235 240 245 atc aac cac ctc ttc cac atc gtc ttc gtg gga gac acc tcc cat atg 883 Ile Asn His Leu Phe His Ile Val Phe Val Gly Asp Thr Ser His Met 250 255 260 tcc gga tcc agc gct ggt ttg ggc ggt ttc aag aca gca ctc gca cac 931 Ser Gly Ser Ser Ala Gly Leu Gly Gly Phe Lys Thr Ala Leu Ala His 265 270 275 ctt ggc att att gaa tcc aat gcg atg gca gtt cct cac cag agc ctc 979 Leu Gly Ile Ile Glu Ser Asn Ala Met Ala Val Pro His Gln Ser Leu 280 285 290 agc gac gaa gaa act gct cgc att cac gcc att gtt gat gaa ttc ctg 1027 Ser Asp Glu Glu Thr Ala Arg Ile His Ala Ile Val Asp Glu Phe Leu 295 300 305 tac acc gct taaggcccac acctcatgac tga 1059 Tyr Thr Ala 310 32 312 PRT Corynebacterium glutamicum 32 Met Ala Ser Ala Thr Phe Thr Gly Val Ile Pro Pro Val Met Thr Pro 1 5 10 15 Leu His Ala Asp Gly Ser Val Asp Val Glu Ser Leu Arg Lys Leu Val 20 25 30 Asp His Leu Ile Asn Gly Gly Val Asp Gly Leu Phe Ala Leu Gly Ser 35 40 45 Ser Gly Glu Ala Ala Phe Leu Thr Arg Ala Gln Arg Lys Leu Ala Leu 50 55 60 Thr Thr Ile Ile Glu His Thr Ala Gly Arg Val Pro Val Thr Ala Gly 65 70 75 80 Val Ile Glu Thr Thr Thr Ala Arg Val Ile Glu Leu Val Glu Asp Ala 85 90 95 Leu Glu Ala Gly Ala Glu Gly Leu Val Ala Thr Ala Pro Phe Tyr Thr 100 105 110 Arg Thr His Asp Val Glu Ile Glu Glu His Phe Arg Lys Ile His Ala 115 120 125 Ala Ala Pro Glu Leu Pro Leu Phe Ala Tyr Asn Ile Pro Val Ser Val 130 135 140 His Ser Asn Leu Asn Pro Val Met Leu Leu Thr Leu Ala Lys Asp Gly 145 150 155 160 Val Leu Ala Gly Thr Lys Asp Ser Ser Gly Asn Asp Gly Ala Ile Arg 165 170 175 Ser Leu Ile Glu Ala Arg Asp Asp Ala Gly Leu Thr Glu Gln Phe Lys 180 185 190 Ile Leu Thr Gly Ser Glu Thr Thr Val Asp Phe Ala Tyr Leu Ala Gly 195 200 205 Ala Asp Gly Val Val Pro Gly Leu Gly Asn Val Asp Pro Ala Ala Tyr 210 215 220 Ala Ala Leu Ala Lys Leu Cys Leu Asp Gly Lys Trp Ala Glu Ala Ala 225 230 235 240 Ala Leu Gln Lys Arg Ile Asn His Leu Phe His Ile Val Phe Val Gly 245 250 255 Asp Thr Ser His Met Ser Gly Ser Ser Ala Gly Leu Gly Gly Phe Lys 260 265 270 Thr Ala Leu Ala His Leu Gly Ile Ile Glu Ser Asn Ala Met Ala Val 275 280 285 Pro His Gln Ser Leu Ser Asp Glu Glu Thr Ala Arg Ile His Ala Ile 290 295 300 Val Asp Glu Phe Leu Tyr Thr Ala 305 310 33 867 DNA Corynebacterium glutamicum CDS (101)..(844) RXA00863 33 aacggtcagt taggtatgga tatcagcacc ttctgaacgg gtacgtctag actggtgggc 60 gtttgaaaaa ctcttcgccc cacgaaaatg aaggagcata atg gga atc aag gtt 115 Met Gly Ile Lys Val 1 5 ggc gtt ctc gga gcc aaa ggc cgt gtt ggt caa act att gtg gca gca 163 Gly Val Leu Gly Ala Lys Gly Arg Val Gly Gln Thr Ile Val Ala Ala 10 15 20 gtc aat gag tcc gac gat ctg gag ctt gtt gca gag atc ggc gtc gac 211 Val Asn Glu Ser Asp Asp Leu Glu Leu Val Ala Glu Ile Gly Val Asp 25 30 35 gat gat ttg agc ctt ctg gta gac aac ggc gct gaa gtt gtc gtt gac 259 Asp Asp Leu Ser Leu Leu Val Asp Asn Gly Ala Glu Val Val Val Asp 40 45 50 ttc acc act cct aac gct gtg atg ggc aac ctg gag ttc tgc atc aac 307 Phe Thr Thr Pro Asn Ala Val Met Gly Asn Leu Glu Phe Cys Ile Asn 55 60 65 aac ggc att tct gcg gtt gtt gga acc acg ggc ttc gat gat gct cgt 355 Asn Gly Ile Ser Ala Val Val Gly Thr Thr Gly Phe Asp Asp Ala Arg 70 75 80 85 ttg gag cag gtt cgc gac tgg ctt gaa gga aaa gac aat gtc ggt gtt 403 Leu Glu Gln Val Arg Asp Trp Leu Glu Gly Lys Asp Asn Val Gly Val 90 95 100 ctg atc gca cct aac ttt gct atc tct gcg gtg ttg acc atg gtc ttt 451 Leu Ile Ala Pro Asn Phe Ala Ile Ser Ala Val Leu Thr Met Val Phe 105 110 115 tcc aag cag gct gcc cgc ttc ttc gaa tca gct gaa gtt att gag ctg 499 Ser Lys Gln Ala Ala Arg Phe Phe Glu Ser Ala Glu Val Ile Glu Leu 120 125 130 cac cac ccc aac aag ctg gat gca cct tca ggc acc gcg atc cac act 547 His His Pro Asn Lys Leu Asp Ala Pro Ser Gly Thr Ala Ile His Thr 135 140 145 gct cag ggc att gct gcg gca cgc aaa gaa gca ggc atg gac gca cag 595 Ala Gln Gly Ile Ala Ala Ala Arg Lys Glu Ala Gly Met Asp Ala Gln 150 155 160 165 cca gat gcg acc gag cag gca ctt gag ggt tcc cgt ggc gca agc gta 643 Pro Asp Ala Thr Glu Gln Ala Leu Glu Gly Ser Arg Gly Ala Ser Val 170 175 180 gat gga atc ccg gtt cat gca gtc cgc atg tcc ggc atg gtt gct cac 691 Asp Gly Ile Pro Val His Ala Val Arg Met Ser Gly Met Val Ala His 185 190 195 gag caa gtt atc ttt ggc acc cag ggt cag acc ttg acc atc aag cag 739 Glu Gln Val Ile Phe Gly Thr Gln Gly Gln Thr Leu Thr Ile Lys Gln 200 205 210 gac tcc tat gat cgc aac tca ttt gca cca ggt gtc ttg gtg ggt gtg 787 Asp Ser Tyr Asp Arg Asn Ser Phe Ala Pro Gly Val Leu Val Gly Val 215 220 225 cgc aac att gca cag cac cca ggc cta gtc gta gga ctt gag cat tac 835 Arg Asn Ile Ala Gln His Pro Gly Leu Val Val Gly Leu Glu His Tyr 230 235 240 245 cta ggc ctg taaaggctca tttcagcagc ggg 867 Leu Gly Leu 34 248 PRT Corynebacterium glutamicum 34 Met Gly Ile Lys Val Gly Val Leu Gly Ala Lys Gly Arg Val Gly Gln 1 5 10 15 Thr Ile Val Ala Ala Val Asn Glu Ser Asp Asp Leu Glu Leu Val Ala 20 25 30 Glu Ile Gly Val Asp Asp Asp Leu Ser Leu Leu Val Asp Asn Gly Ala 35 40 45 Glu Val Val Val Asp Phe Thr Thr Pro Asn Ala Val Met Gly Asn Leu 50 55 60 Glu Phe Cys Ile Asn Asn Gly Ile Ser Ala Val Val Gly Thr Thr Gly 65 70 75 80 Phe Asp Asp Ala Arg Leu Glu Gln Val Arg Asp Trp Leu Glu Gly Lys 85 90 95 Asp Asn Val Gly Val Leu Ile Ala Pro Asn Phe Ala Ile Ser Ala Val 100 105 110 Leu Thr Met Val Phe Ser Lys Gln Ala Ala Arg Phe Phe Glu Ser Ala 115 120 125 Glu Val Ile Glu Leu His His Pro Asn Lys Leu Asp Ala Pro Ser Gly 130 135 140 Thr Ala Ile His Thr Ala Gln Gly Ile Ala Ala Ala Arg Lys Glu Ala 145 150 155 160 Gly Met Asp Ala Gln Pro Asp Ala Thr Glu Gln Ala Leu Glu Gly Ser 165 170 175 Arg Gly Ala Ser Val Asp Gly Ile Pro Val His Ala Val Arg Met Ser 180 185 190 Gly Met Val Ala His Glu Gln Val Ile Phe Gly Thr Gln Gly Gln Thr 195 200 205 Leu Thr Ile Lys Gln Asp Ser Tyr Asp Arg Asn Ser Phe Ala Pro Gly 210 215 220 Val Leu Val Gly Val Arg Asn Ile Ala Gln His Pro Gly Leu Val Val 225 230 235 240 Gly Leu Glu His Tyr Leu Gly Leu 245 35 873 DNA Corynebacterium glutamicum CDS (101)..(850) RXA00864 35 acagcaccca ggcctagtcg taggacttga gcattaccta ggcctgtaaa ggctcatttc 60 agcagcgggt ggaatttttt aaaaggagcg tttaaaggct gtg gcc gaa caa gtt 115 Val Ala Glu Gln Val 1 5 aaa ttg agc gtg gag ttg ata gcg tgc agt tct ttt act cca ccc gct 163 Lys Leu Ser Val Glu Leu Ile Ala Cys Ser Ser Phe Thr Pro Pro Ala 10 15 20 gat gtt gag tgg tca act gat gtt gag ggc gcg gaa gca ctc gtc gag 211 Asp Val Glu Trp Ser Thr Asp Val Glu Gly Ala Glu Ala Leu Val Glu 25 30 35 ttt gcg ggt cgt gcc tgc tac gaa act ttt gat aag ccg aac cct cga 259 Phe Ala Gly Arg Ala Cys Tyr Glu Thr Phe Asp Lys Pro Asn Pro Arg 40 45 50 act gct tcc aat gct gcg tat ctg cgc cac atc atg gaa gtg ggg cac 307 Thr Ala Ser Asn Ala Ala Tyr Leu Arg His Ile Met Glu Val Gly His 55 60 65 act gct ttg ctt gag cat gcc aat gcc acg atg tat atc cga ggc att 355 Thr Ala Leu Leu Glu His Ala Asn Ala Thr Met Tyr Ile Arg Gly Ile 70 75 80 85 tct cgg tcc gcg acc cat gaa ttg gtc cga cac cgc cat ttt tcc ttc 403 Ser Arg Ser Ala Thr His Glu Leu Val Arg His Arg His Phe Ser Phe 90 95 100 tct caa ctg tct cag cgt ttc gtg cac agc gga gaa tcg gaa gta gtg 451 Ser Gln Leu Ser Gln Arg Phe Val His Ser Gly Glu Ser Glu Val Val 105 110 115 gtg ccc act ctc atc gat gaa gat ccg cag ttg cgt gaa ctt ttc atg 499 Val Pro Thr Leu Ile Asp Glu Asp Pro Gln Leu Arg Glu Leu Phe Met 120 125 130 cac gcc atg gat gag tct cgg ttc gct ttc aat gag ctg ctt aat gcg 547 His Ala Met Asp Glu Ser Arg Phe Ala Phe Asn Glu Leu Leu Asn Ala 135 140 145 ctg gaa gaa aaa ctt ggc gat gaa ccg aat gca ctt tta agg aaa aag 595 Leu Glu Glu Lys Leu Gly Asp Glu Pro Asn Ala Leu Leu Arg Lys Lys 150 155 160 165 cag gct cgt caa gca gct cgc gct gtg ctg ccc aac gct aca gag tcc 643 Gln Ala Arg Gln Ala Ala Arg Ala Val Leu Pro Asn Ala Thr Glu Ser 170 175 180 aga atc gtg gtg tct gga aac ttc cgc acc tgg agg cat ttc att ggc 691 Arg Ile Val Val Ser Gly Asn Phe Arg Thr Trp Arg His Phe Ile Gly 185 190 195 atg cga gcc agt gaa cat gca gac gtc gaa atc cgc gaa gta gcg gta 739 Met Arg Ala Ser Glu His Ala Asp Val Glu Ile Arg Glu Val Ala Val 200 205 210 gaa tgt tta aga aag ctg cag gta gca gcg cca act gtt ttc ggt gat 787 Glu Cys Leu Arg Lys Leu Gln Val Ala Ala Pro Thr Val Phe Gly Asp 215 220 225 ttt gag att gaa act ttg gca gac gga tcg caa atg gca aca agc ccg 835 Phe Glu Ile Glu Thr Leu Ala Asp Gly Ser Gln Met Ala Thr Ser Pro 230 235 240 245 tat gtc atg gac ttt taacgcaaag ctcacaccca cga 873 Tyr Val Met Asp Phe 250 36 250 PRT Corynebacterium glutamicum 36 Val Ala Glu Gln Val Lys Leu Ser Val Glu Leu Ile Ala Cys Ser Ser 1 5 10 15 Phe Thr Pro Pro Ala Asp Val Glu Trp Ser Thr Asp Val Glu Gly Ala 20 25 30 Glu Ala Leu Val Glu Phe Ala Gly Arg Ala Cys Tyr Glu Thr Phe Asp 35 40 45 Lys Pro Asn Pro Arg Thr Ala Ser Asn Ala Ala Tyr Leu Arg His Ile 50 55 60 Met Glu Val Gly His Thr Ala Leu Leu Glu His Ala Asn Ala Thr Met 65 70 75 80 Tyr Ile Arg Gly Ile Ser Arg Ser Ala Thr His Glu Leu Val Arg His 85 90 95 Arg His Phe Ser Phe Ser Gln Leu Ser Gln Arg Phe Val His Ser Gly 100 105 110 Glu Ser Glu Val Val Val Pro Thr Leu Ile Asp Glu Asp Pro Gln Leu 115 120 125 Arg Glu Leu Phe Met His Ala Met Asp Glu Ser Arg Phe Ala Phe Asn 130 135 140 Glu Leu Leu Asn Ala Leu Glu Glu Lys Leu Gly Asp Glu Pro Asn Ala 145 150 155 160 Leu Leu Arg Lys Lys Gln Ala Arg Gln Ala Ala Arg Ala Val Leu Pro 165 170 175 Asn Ala Thr Glu Ser Arg Ile Val Val Ser Gly Asn Phe Arg Thr Trp 180 185 190 Arg His Phe Ile Gly Met Arg Ala Ser Glu His Ala Asp Val Glu Ile 195 200 205 Arg Glu Val Ala Val Glu Cys Leu Arg Lys Leu Gln Val Ala Ala Pro 210 215 220 Thr Val Phe Gly Asp Phe Glu Ile Glu Thr Leu Ala Asp Gly Ser Gln 225 230 235 240 Met Ala Thr Ser Pro Tyr Val Met Asp Phe 245 250 37 608 DNA Corynebacterium glutamicum CDS (69)..(608) RXA02843 37 cccattgcgc ggaggtcgca ccccttccga cttgaactga taggccgata gaaattattc 60 tggacgtc atg act act gct tcc gca acc gga att gca aca ctg acc tcc 110 Met Thr Thr Ala Ser Ala Thr Gly Ile Ala Thr Leu Thr Ser 1 5 10 acc ggc gac gtc ctg gac gtg tgg tat cca gaa atc ggg tcc acc gac 158 Thr Gly Asp Val Leu Asp Val Trp Tyr Pro Glu Ile Gly Ser Thr Asp 15 20 25 30 cag tcc gcg ctc aca cct cta gaa ggc gtc gat gaa gat cga aac gtc 206 Gln Ser Ala Leu Thr Pro Leu Glu Gly Val Asp Glu Asp Arg Asn Val 35 40 45 acc cgc aaa atc gtg acg aca act atc gac acc gac gca gcc ccc acc 254 Thr Arg Lys Ile Val Thr Thr Thr Ile Asp Thr Asp Ala Ala Pro Thr 50 55 60 gac acc tac gat gca tgg ctg cgc ctt cac ctc ctc tcc cac cgc gtt 302 Asp Thr Tyr Asp Ala Trp Leu Arg Leu His Leu Leu Ser His Arg Val 65 70 75 ttc cgc cct cac acc atc aac cta gac ggc att ttc ggc ctc ctc aac 350 Phe Arg Pro His Thr Ile Asn Leu Asp Gly Ile Phe Gly Leu Leu Asn 80 85 90 aat gtc gtg tgg acc aac ttc gga ccg tgc gca gtt gac ggt ttc gca 398 Asn Val Val Trp Thr Asn Phe Gly Pro Cys Ala Val Asp Gly Phe Ala 95 100 105 110 ctc acc cgc gcg cgc ctg tca cgc cga ggc caa gtt acg gtt tat agc 446 Leu Thr Arg Ala Arg Leu Ser Arg Arg Gly Gln Val Thr Val Tyr Ser 115 120 125 gtc gac aag ttc cca cgc atg gtc gac tat gtg gtt ccc tcg ggc gtg 494 Val Asp Lys Phe Pro Arg Met Val Asp Tyr Val Val Pro Ser Gly Val 130 135 140 cgc atc ggt gac gcc gac cgc gtc cga ctt ggc gcg tac ctg gca gat 542 Arg Ile Gly Asp Ala Asp Arg Val Arg Leu Gly Ala Tyr Leu Ala Asp 145 150 155 ggc acc acc gtg atg cat gag ggc ttc gtg aac ttc aac gct ggc acg 590 Gly Thr Thr Val Met His Glu Gly Phe Val Asn Phe Asn Ala Gly Thr 160 165 170 ctc ggc gct tcc atg gtt 608 Leu Gly Ala Ser Met Val 175 180 38 180 PRT Corynebacterium glutamicum 38 Met Thr Thr Ala Ser Ala Thr Gly Ile Ala Thr Leu Thr Ser Thr Gly 1 5 10 15 Asp Val Leu Asp Val Trp Tyr Pro Glu Ile Gly Ser Thr Asp Gln Ser 20 25 30 Ala Leu Thr Pro Leu Glu Gly Val Asp Glu Asp Arg Asn Val Thr Arg 35 40 45 Lys Ile Val Thr Thr Thr Ile Asp Thr Asp Ala Ala Pro Thr Asp Thr 50 55 60 Tyr Asp Ala Trp Leu Arg Leu His Leu Leu Ser His Arg Val Phe Arg 65 70 75 80 Pro His Thr Ile Asn Leu Asp Gly Ile Phe Gly Leu Leu Asn Asn Val 85 90 95 Val Trp Thr Asn Phe Gly Pro Cys Ala Val Asp Gly Phe Ala Leu Thr 100 105 110 Arg Ala Arg Leu Ser Arg Arg Gly Gln Val Thr Val Tyr Ser Val Asp 115 120 125 Lys Phe Pro Arg Met Val Asp Tyr Val Val Pro Ser Gly Val Arg Ile 130 135 140 Gly Asp Ala Asp Arg Val Arg Leu Gly Ala Tyr Leu Ala Asp Gly Thr 145 150 155 160 Thr Val Met His Glu Gly Phe Val Asn Phe Asn Ala Gly Thr Leu Gly 165 170 175 Ala Ser Met Val 180 39 1143 DNA Corynebacterium glutamicum CDS (101)..(1120) RXN00355 39 aatagatcag cgcatccgtg gtggaaccaa aaggctcaac aatacgaaac gttcgctttc 60 ggtcctgatg aaagagatgt ccctgaatca tcatctaagt atg cat ctc ggt aag 115 Met His Leu Gly Lys 1 5 ctc gac cag gac agt gcc acc aca att ttg gag gat tac aag aac atg 163 Leu Asp Gln Asp Ser Ala Thr Thr Ile Leu Glu Asp Tyr Lys Asn Met 10 15 20 acc aac atc cgc gta gct atc gtg ggc tac gga aac ctg gga cgc agc 211 Thr Asn Ile Arg Val Ala Ile Val Gly Tyr Gly Asn Leu Gly Arg Ser 25 30 35 gtc gaa aag ctt att gcc aag cag ccc gac atg gac ctt gta gga atc 259 Val Glu Lys Leu Ile Ala Lys Gln Pro Asp Met Asp Leu Val Gly Ile 40 45 50 ttc tcg cgc cgg gcc acc ctc gac aca aag acg cca gtc ttt gat gtc 307 Phe Ser Arg Arg Ala Thr Leu Asp Thr Lys Thr Pro Val Phe Asp Val 55 60 65 gcc gac gtg gac aag cac gcc gac gac gtg gac gtg ctg ttc ctg tgc 355 Ala Asp Val Asp Lys His Ala Asp Asp Val Asp Val Leu Phe Leu Cys 70 75 80 85 atg ggc tcc gcc acc gac atc cct gag cag gca cca aag ttc gcg cag 403 Met Gly Ser Ala Thr Asp Ile Pro Glu Gln Ala Pro Lys Phe Ala Gln 90 95 100 ttc gcc tgc acc gta gac acc tac gac aac cac cgc gac atc cca cgc 451 Phe Ala Cys Thr Val Asp Thr Tyr Asp Asn His Arg Asp Ile Pro Arg 105 110 115 cac cgc cag gtc atg aac gaa gcc gcc acc gca gcc ggc aac gtt gca 499 His Arg Gln Val Met Asn Glu Ala Ala Thr Ala Ala Gly Asn Val Ala 120 125 130 ctg gtc tct acc ggc tgg gat cca gga atg ttc tcc atc aac cgc gtc 547 Leu Val Ser Thr Gly Trp Asp Pro Gly Met Phe Ser Ile Asn Arg Val 135 140 145 tac gca gcg gca gtc tta gcc gag cac cag cag cac acc ttc tgg ggc 595 Tyr Ala Ala Ala Val Leu Ala Glu His Gln Gln His Thr Phe Trp Gly 150 155 160 165 cca ggt ttg tca cag ggc cac tcc gat gct ttg cga cgc atc cct ggc 643 Pro Gly Leu Ser Gln Gly His Ser Asp Ala Leu Arg Arg Ile Pro Gly 170 175 180 gtt caa aag gca gtc cag tac acc ctc cca tcc gaa gac gcc ctg gaa 691 Val Gln Lys Ala Val Gln Tyr Thr Leu Pro Ser Glu Asp Ala Leu Glu 185 190 195 aag gcc cgc cgc ggc gaa gcc ggc gac ctt acc gga aag caa acc cac 739 Lys Ala Arg Arg Gly Glu Ala Gly Asp Leu Thr Gly Lys Gln Thr His 200 205 210 aag cgc caa tgc ttc gtg gtt gcc gac gcg gcc gat cac gag cgc atc 787 Lys Arg Gln Cys Phe Val Val Ala Asp Ala Ala Asp His Glu Arg Ile 215 220 225 gaa aac gac atc cgc acc atg cct gat tac ttc gtt ggc tac gaa gtc 835 Glu Asn Asp Ile Arg Thr Met Pro Asp Tyr Phe Val Gly Tyr Glu Val 230 235 240 245 gaa gtc aac ttc atc gac gaa gca acc ttc gac tcc gag cac acc ggc 883 Glu Val Asn Phe Ile Asp Glu Ala Thr Phe Asp Ser Glu His Thr Gly 250 255 260 atg cca cac ggt ggc cac gtg att acc acc ggc gac acc ggt ggc ttc 931 Met Pro His Gly Gly His Val Ile Thr Thr Gly Asp Thr Gly Gly Phe 265 270 275 aac cac acc gtg gaa tac atc ctc aag ctg gac cga aac cca gat ttc 979 Asn His Thr Val Glu Tyr Ile Leu Lys Leu Asp Arg Asn Pro Asp Phe 280 285 290 acc gct tcc tca cag atc gct ttc ggt cgc gca gct cac cgc atg aag 1027 Thr Ala Ser Ser Gln Ile Ala Phe Gly Arg Ala Ala His Arg Met Lys 295 300 305 cag cag ggc caa agc gga gct ttc acc gtc ctc gaa gtt gct cca tac 1075 Gln Gln Gly Gln Ser Gly Ala Phe Thr Val Leu Glu Val Ala Pro Tyr 310 315 320 325 ctg ctc tcc cca gag aac ttg gac gat ctg atc gca cgc gac gtc 1120 Leu Leu Ser Pro Glu Asn Leu Asp Asp Leu Ile Ala Arg Asp Val 330 335 340 taatttagct cgaggggcaa gga 1143 40 340 PRT Corynebacterium glutamicum 40 Met His Leu Gly Lys Leu Asp Gln Asp Ser Ala Thr Thr Ile Leu Glu 1 5 10 15 Asp Tyr Lys Asn Met Thr Asn Ile Arg Val Ala Ile Val Gly Tyr Gly 20 25 30 Asn Leu Gly Arg Ser Val Glu Lys Leu Ile Ala Lys Gln Pro Asp Met 35 40 45 Asp Leu Val Gly Ile Phe Ser Arg Arg Ala Thr Leu Asp Thr Lys Thr 50 55 60 Pro Val Phe Asp Val Ala Asp Val Asp Lys His Ala Asp Asp Val Asp 65 70 75 80 Val Leu Phe Leu Cys Met Gly Ser Ala Thr Asp Ile Pro Glu Gln Ala 85 90 95 Pro Lys Phe Ala Gln Phe Ala Cys Thr Val Asp Thr Tyr Asp Asn His 100 105 110 Arg Asp Ile Pro Arg His Arg Gln Val Met Asn Glu Ala Ala Thr Ala 115 120 125 Ala Gly Asn Val Ala Leu Val Ser Thr Gly Trp Asp Pro Gly Met Phe 130 135 140 Ser Ile Asn Arg Val Tyr Ala Ala Ala Val Leu Ala Glu His Gln Gln 145 150 155 160 His Thr Phe Trp Gly Pro Gly Leu Ser Gln Gly His Ser Asp Ala Leu 165 170 175 Arg Arg Ile Pro Gly Val Gln Lys Ala Val Gln Tyr Thr Leu Pro Ser 180 185 190 Glu Asp Ala Leu Glu Lys Ala Arg Arg Gly Glu Ala Gly Asp Leu Thr 195 200 205 Gly Lys Gln Thr His Lys Arg Gln Cys Phe Val Val Ala Asp Ala Ala 210 215 220 Asp His Glu Arg Ile Glu Asn Asp Ile Arg Thr Met Pro Asp Tyr Phe 225 230 235 240 Val Gly Tyr Glu Val Glu Val Asn Phe Ile Asp Glu Ala Thr Phe Asp 245 250 255 Ser Glu His Thr Gly Met Pro His Gly Gly His Val Ile Thr Thr Gly 260 265 270 Asp Thr Gly Gly Phe Asn His Thr Val Glu Tyr Ile Leu Lys Leu Asp 275 280 285 Arg Asn Pro Asp Phe Thr Ala Ser Ser Gln Ile Ala Phe Gly Arg Ala 290 295 300 Ala His Arg Met Lys Gln Gln Gly Gln Ser Gly Ala Phe Thr Val Leu 305 310 315 320 Glu Val Ala Pro Tyr Leu Leu Ser Pro Glu Asn Leu Asp Asp Leu Ile 325 330 335 Ala Arg Asp Val 340 41 958 DNA Corynebacterium glutamicum CDS (101)..(958) FRXA00352 41 aatagatcag cgcatccgtg gtggaaccaa aaggctcaac aatacgaaac gttcgctttc 60 ggtcctgatg aaagagatgt ccctgaatca tcatctaagt atg cat ctc ggt aag 115 Met His Leu Gly Lys 1 5 ctc gac cag gac agt gcc acc aca att ttg gag gat tac aag aac atg 163 Leu Asp Gln Asp Ser Ala Thr Thr Ile Leu Glu Asp Tyr Lys Asn Met 10 15 20 acc aac atc cgc gta gct atc gtg ggc tac gga aac ctg gga cgc agc 211 Thr Asn Ile Arg Val Ala Ile Val Gly Tyr Gly Asn Leu Gly Arg Ser 25 30 35 gtc gaa aag ctt att gcc aag cag ccc gac atg gac ctt gta gga atc 259 Val Glu Lys Leu Ile Ala Lys Gln Pro Asp Met Asp Leu Val Gly Ile 40 45 50 ttc tcg cgc cgg gcc acc ctc gac aca aag acg cca gtc ttt gat gtc 307 Phe Ser Arg Arg Ala Thr Leu Asp Thr Lys Thr Pro Val Phe Asp Val 55 60 65 gcc gac gtg gac aag cac gcc gac gac gtg gac gtg ctg ttc ctg tgc 355 Ala Asp Val Asp Lys His Ala Asp Asp Val Asp Val Leu Phe Leu Cys 70 75 80 85 atg ggc tcc gcc acc gac atc cct gag cag gca cca aag ttc gcg cag 403 Met Gly Ser Ala Thr Asp Ile Pro Glu Gln Ala Pro Lys Phe Ala Gln 90 95 100 ttc gcc tgc acc gta gac acc tac gac aac cac cgc gac atc cca cgc 451 Phe Ala Cys Thr Val Asp Thr Tyr Asp Asn His Arg Asp Ile Pro Arg 105 110 115 cac cgc cag gtc atg aac gaa gcc gcc acc gca gcc ggc aac gtt gca 499 His Arg Gln Val Met Asn Glu Ala Ala Thr Ala Ala Gly Asn Val Ala 120 125 130 ctg gtc tct acc ggc tgg gat cca gga atg ttc tcc atc aac cgc gtc 547 Leu Val Ser Thr Gly Trp Asp Pro Gly Met Phe Ser Ile Asn Arg Val 135 140 145 tac gca gcg gca gtc tta gcc gag cac cag cag cac acc ttc tgg ggc 595 Tyr Ala Ala Ala Val Leu Ala Glu His Gln Gln His Thr Phe Trp Gly 150 155 160 165 cca ggt ttg tca cag ggc cac tcc gat gct ttg cga cgc atc cct ggc 643 Pro Gly Leu Ser Gln Gly His Ser Asp Ala Leu Arg Arg Ile Pro Gly 170 175 180 gtt caa aag gca gtc cag tac acc ctc cca tcc gaa gac gcc ctg gaa 691 Val Gln Lys Ala Val Gln Tyr Thr Leu Pro Ser Glu Asp Ala Leu Glu 185 190 195 aag gcc cgc cgc ggc gaa gcc ggc gac ctt acc gga aag caa acc cac 739 Lys Ala Arg Arg Gly Glu Ala Gly Asp Leu Thr Gly Lys Gln Thr His 200 205 210 aag cgc caa tgc ttc gtg gtt gcc gac gcg gcc gat cac gag cgc atc 787 Lys Arg Gln Cys Phe Val Val Ala Asp Ala Ala Asp His Glu Arg Ile 215 220 225 gaa aac gac atc cgc acc atg cct gat tac ttc gtt ggc tac gaa gtc 835 Glu Asn Asp Ile Arg Thr Met Pro Asp Tyr Phe Val Gly Tyr Glu Val 230 235 240 245 gaa gtc aac ttc atc gac gaa gca acc ttc gac tcc gag cac acc ggc 883 Glu Val Asn Phe Ile Asp Glu Ala Thr Phe Asp Ser Glu His Thr Gly 250 255 260 atg cca cac ggt ggc cac gtg att acc acc ggc gac acc ggt ggc ttc 931 Met Pro His Gly Gly His Val Ile Thr Thr Gly Asp Thr Gly Gly Phe 265 270 275 aac cac acc gtg gaa tac atc ctc aag 958 Asn His Thr Val Glu Tyr Ile Leu Lys 280 285 42 286 PRT Corynebacterium glutamicum 42 Met His Leu Gly Lys Leu Asp Gln Asp Ser Ala Thr Thr Ile Leu Glu 1 5 10 15 Asp Tyr Lys Asn Met Thr Asn Ile Arg Val Ala Ile Val Gly Tyr Gly 20 25 30 Asn Leu Gly Arg Ser Val Glu Lys Leu Ile Ala Lys Gln Pro Asp Met 35 40 45 Asp Leu Val Gly Ile Phe Ser Arg Arg Ala Thr Leu Asp Thr Lys Thr 50 55 60 Pro Val Phe Asp Val Ala Asp Val Asp Lys His Ala Asp Asp Val Asp 65 70 75 80 Val Leu Phe Leu Cys Met Gly Ser Ala Thr Asp Ile Pro Glu Gln Ala 85 90 95 Pro Lys Phe Ala Gln Phe Ala Cys Thr Val Asp Thr Tyr Asp Asn His 100 105 110 Arg Asp Ile Pro Arg His Arg Gln Val Met Asn Glu Ala Ala Thr Ala 115 120 125 Ala Gly Asn Val Ala Leu Val Ser Thr Gly Trp Asp Pro Gly Met Phe 130 135 140 Ser Ile Asn Arg Val Tyr Ala Ala Ala Val Leu Ala Glu His Gln Gln 145 150 155 160 His Thr Phe Trp Gly Pro Gly Leu Ser Gln Gly His Ser Asp Ala Leu 165 170 175 Arg Arg Ile Pro Gly Val Gln Lys Ala Val Gln Tyr Thr Leu Pro Ser 180 185 190 Glu Asp Ala Leu Glu Lys Ala Arg Arg Gly Glu Ala Gly Asp Leu Thr 195 200 205 Gly Lys Gln Thr His Lys Arg Gln Cys Phe Val Val Ala Asp Ala Ala 210 215 220 Asp His Glu Arg Ile Glu Asn Asp Ile Arg Thr Met Pro Asp Tyr Phe 225 230 235 240 Val Gly Tyr Glu Val Glu Val Asn Phe Ile Asp Glu Ala Thr Phe Asp 245 250 255 Ser Glu His Thr Gly Met Pro His Gly Gly His Val Ile Thr Thr Gly 260 265 270 Asp Thr Gly Gly Phe Asn His Thr Val Glu Tyr Ile Leu Lys 275 280 285 43 1400 DNA Corynebacterium glutamicum CDS (1)..(1377) RXA00972 43 cct gca cct ggt tgg cgt ttc cgc acc gga gaa gat gta aca atg gct 48 Pro Ala Pro Gly Trp Arg Phe Arg Thr Gly Glu Asp Val Thr Met Ala 1 5 10 15 aca gtt gaa aat ttc aat gaa ctt ccc gca cac gta tgg cca cgc aat 96 Thr Val Glu Asn Phe Asn Glu Leu Pro Ala His Val Trp Pro Arg Asn 20 25 30 gcc gtg cgc caa gaa gac ggc gtt gtc acc gtc gct ggt gtg cct ctg 144 Ala Val Arg Gln Glu Asp Gly Val Val Thr Val Ala Gly Val Pro Leu 35 40 45 cct gac ctc gct gaa gaa tac gga acc cca ctg ttc gta gtc gac gag 192 Pro Asp Leu Ala Glu Glu Tyr Gly Thr Pro Leu Phe Val Val Asp Glu 50 55 60 gac gat ttc cgt tcc cgc tgt cgc gac atg gct acc gca ttc ggt gga 240 Asp Asp Phe Arg Ser Arg Cys Arg Asp Met Ala Thr Ala Phe Gly Gly 65 70 75 80 cca ggc aat gtg cac tac gca tct aaa gcg ttc ctg acc aag acc att 288 Pro Gly Asn Val His Tyr Ala Ser Lys Ala Phe Leu Thr Lys Thr Ile 85 90 95 gca cgt tgg gtt gat gaa gag ggg ctg gca ctg gac att gca tcc atc 336 Ala Arg Trp Val Asp Glu Glu Gly Leu Ala Leu Asp Ile Ala Ser Ile 100 105 110 aac gaa ctg ggc att gcc ctg gcc gct ggt ttc ccc gcc agc cgt atc 384 Asn Glu Leu Gly Ile Ala Leu Ala Ala Gly Phe Pro Ala Ser Arg Ile 115 120 125 acc gcg cac ggc aac aac aaa ggc gta gag ttc ctg cgc gcg ttg gtt 432 Thr Ala His Gly Asn Asn Lys Gly Val Glu Phe Leu Arg Ala Leu Val 130 135 140 caa aac ggt gtg gga cac gtg gtg ctg gac tcc gca cag gaa cta gaa 480 Gln Asn Gly Val Gly His Val Val Leu Asp Ser Ala Gln Glu Leu Glu 145 150 155 160 ctg ttg gat tac gtt gcc gct ggt gaa ggc aag att cag gac gtg ttg 528 Leu Leu Asp Tyr Val Ala Ala Gly Glu Gly Lys Ile Gln Asp Val Leu 165 170 175 atc cgc gta aag cca ggc atc gaa gca cac acc cac gag ttc atc gcc 576 Ile Arg Val Lys Pro Gly Ile Glu Ala His Thr His Glu Phe Ile Ala 180 185 190 act agc cac gaa gac cag aag ttc gga ttc tcc ctg gca tcc ggt tcc 624 Thr Ser His Glu Asp Gln Lys Phe Gly Phe Ser Leu Ala Ser Gly Ser 195 200 205 gca ttc gaa gca gca aaa gcc gcc aac aac gca gaa aac ctg aac ctg 672 Ala Phe Glu Ala Ala Lys Ala Ala Asn Asn Ala Glu Asn Leu Asn Leu 210 215 220 gtt ggc ctg cac tgc cac gtt ggt tcc cag gtg ttc gac gcc gaa ggc 720 Val Gly Leu His Cys His Val Gly Ser Gln Val Phe Asp Ala Glu Gly 225 230 235 240 ttc aag ctg gca gca gaa cgc gtg ttg ggc ctg tac tca cag atc cac 768 Phe Lys Leu Ala Ala Glu Arg Val Leu Gly Leu Tyr Ser Gln Ile His 245 250 255 agc gaa ctg ggc gtt gcc ctt cct gaa ctg gat ctc ggt ggc gga tac 816 Ser Glu Leu Gly Val Ala Leu Pro Glu Leu Asp Leu Gly Gly Gly Tyr 260 265 270 ggc att gcc tat acc gca gct gaa gaa cca ctc aac gtc gca gaa gtt 864 Gly Ile Ala Tyr Thr Ala Ala Glu Glu Pro Leu Asn Val Ala Glu Val 275 280 285 gcc tcc gac ctg ctc acc gca gtc gga aaa atg gca gcg gaa cta ggc 912 Ala Ser Asp Leu Leu Thr Ala Val Gly Lys Met Ala Ala Glu Leu Gly 290 295 300 atc gac gca cca acc gtg ctt gtt gag ccc ggc cgc gct atc gca ggc 960 Ile Asp Ala Pro Thr Val Leu Val Glu Pro Gly Arg Ala Ile Ala Gly 305 310 315 320 ccc tcc acc gtg acc atc tac gaa gtc ggc acc acc aaa gac gtc cac 1008 Pro Ser Thr Val Thr Ile Tyr Glu Val Gly Thr Thr Lys Asp Val His 325 330 335 gta gac gac gac aaa acc cgc cgt tac atc gcc gtg gac gga ggc atg 1056 Val Asp Asp Asp Lys Thr Arg Arg Tyr Ile Ala Val Asp Gly Gly Met 340 345 350 tcc gac aac atc cgc cca gca ctc tac ggg tcc gaa tac gac gcc cgc 1104 Ser Asp Asn Ile Arg Pro Ala Leu Tyr Gly Ser Glu Tyr Asp Ala Arg 355 360 365 gta gta tcc cgc ttc gcc gaa gga gac cca gta agc acc cgc atc gtg 1152 Val Val Ser Arg Phe Ala Glu Gly Asp Pro Val Ser Thr Arg Ile Val 370 375 380 ggc tcc cac tgc gaa tcc ggc gat atc ctg atc aac gat gaa atc tac 1200 Gly Ser His Cys Glu Ser Gly Asp Ile Leu Ile Asn Asp Glu Ile Tyr 385 390 395 400 cca tct gac atc acc agc ggc gac ttc ctt gca ctc gca gcc acc ggc 1248 Pro Ser Asp Ile Thr Ser Gly Asp Phe Leu Ala Leu Ala Ala Thr Gly 405 410 415 gca tac tgc tac gcc atg agc tcc cgc tac aac gcc ttc aca cgg ccc 1296 Ala Tyr Cys Tyr Ala Met Ser Ser Arg Tyr Asn Ala Phe Thr Arg Pro 420 425 430 gcc gtc gtg tcc gtc cgc gct ggc agc tcc cgc ctc atg ctg cgc cgc 1344 Ala Val Val Ser Val Arg Ala Gly Ser Ser Arg Leu Met Leu Arg Arg 435 440 445 gaa acg ctc gac gac atc ctc tca cta gag gca taacgctttt cgacgcctga 1397 Glu Thr Leu Asp Asp Ile Leu Ser Leu Glu Ala 450 455 ccc 1400 44 459 PRT Corynebacterium glutamicum 44 Pro Ala Pro Gly Trp Arg Phe Arg Thr Gly Glu Asp Val Thr Met Ala 1 5 10 15 Thr Val Glu Asn Phe Asn Glu Leu Pro Ala His Val Trp Pro Arg Asn 20 25 30 Ala Val Arg Gln Glu Asp Gly Val Val Thr Val Ala Gly Val Pro Leu 35 40 45 Pro Asp Leu Ala Glu Glu Tyr Gly Thr Pro Leu Phe Val Val Asp Glu 50 55 60 Asp Asp Phe Arg Ser Arg Cys Arg Asp Met Ala Thr Ala Phe Gly Gly 65 70 75 80 Pro Gly Asn Val His Tyr Ala Ser Lys Ala Phe Leu Thr Lys Thr Ile 85 90 95 Ala Arg Trp Val Asp Glu Glu Gly Leu Ala Leu Asp Ile Ala Ser Ile 100 105 110 Asn Glu Leu Gly Ile Ala Leu Ala Ala Gly Phe Pro Ala Ser Arg Ile 115 120 125 Thr Ala His Gly Asn Asn Lys Gly Val Glu Phe Leu Arg Ala Leu Val 130 135 140 Gln Asn Gly Val Gly His Val Val Leu Asp Ser Ala Gln Glu Leu Glu 145 150 155 160 Leu Leu Asp Tyr Val Ala Ala Gly Glu Gly Lys Ile Gln Asp Val Leu 165 170 175 Ile Arg Val Lys Pro Gly Ile Glu Ala His Thr His Glu Phe Ile Ala 180 185 190 Thr Ser His Glu Asp Gln Lys Phe Gly Phe Ser Leu Ala Ser Gly Ser 195 200 205 Ala Phe Glu Ala Ala Lys Ala Ala Asn Asn Ala Glu Asn Leu Asn Leu 210 215 220 Val Gly Leu His Cys His Val Gly Ser Gln Val Phe Asp Ala Glu Gly 225 230 235 240 Phe Lys Leu Ala Ala Glu Arg Val Leu Gly Leu Tyr Ser Gln Ile His 245 250 255 Ser Glu Leu Gly Val Ala Leu Pro Glu Leu Asp Leu Gly Gly Gly Tyr 260 265 270 Gly Ile Ala Tyr Thr Ala Ala Glu Glu Pro Leu Asn Val Ala Glu Val 275 280 285 Ala Ser Asp Leu Leu Thr Ala Val Gly Lys Met Ala Ala Glu Leu Gly 290 295 300 Ile Asp Ala Pro Thr Val Leu Val Glu Pro Gly Arg Ala Ile Ala Gly 305 310 315 320 Pro Ser Thr Val Thr Ile Tyr Glu Val Gly Thr Thr Lys Asp Val His 325 330 335 Val Asp Asp Asp Lys Thr Arg Arg Tyr Ile Ala Val Asp Gly Gly Met 340 345 350 Ser Asp Asn Ile Arg Pro Ala Leu Tyr Gly Ser Glu Tyr Asp Ala Arg 355 360 365 Val Val Ser Arg Phe Ala Glu Gly Asp Pro Val Ser Thr Arg Ile Val 370 375 380 Gly Ser His Cys Glu Ser Gly Asp Ile Leu Ile Asn Asp Glu Ile Tyr 385 390 395 400 Pro Ser Asp Ile Thr Ser Gly Asp Phe Leu Ala Leu Ala Ala Thr Gly 405 410 415 Ala Tyr Cys Tyr Ala Met Ser Ser Arg Tyr Asn Ala Phe Thr Arg Pro 420 425 430 Ala Val Val Ser Val Arg Ala Gly Ser Ser Arg Leu Met Leu Arg Arg 435 440 445 Glu Thr Leu Asp Asp Ile Leu Ser Leu Glu Ala 450 455 45 2121 DNA Corynebacterium glutamicum CDS (101)..(2098) RXA02653 45 agacagagtg ttagtgcgtg gggcagctct cactttcatc gacatcactc gagtatgctc 60 accggccgta ttcattccaa taacccgcac agggaaacta atg ata ccg aag ccc 115 Met Ile Pro Lys Pro 1 5 gac gtg acc gac tta tat tta gag gac ctc tta aat gag ggt tcg gaa 163 Asp Val Thr Asp Leu Tyr Leu Glu Asp Leu Leu Asn Glu Gly Ser Glu 10 15 20 aag att cgg tcc gcc aag gat ctt tcc gaa ctt agg aca gtt cta aaa 211 Lys Ile Arg Ser Ala Lys Asp Leu Ser Glu Leu Arg Thr Val Leu Lys 25 30 35 gag gtt tcc tcc caa att cag gaa cga gct ggg aaa aaa gat gaa gaa 259 Glu Val Ser Ser Gln Ile Gln Glu Arg Ala Gly Lys Lys Asp Glu Glu 40 45 50 tgg gga atg ggg gcc act tgg cgg gag ctg tac ccc agc atc gtg gaa 307 Trp Gly Met Gly Ala Thr Trp Arg Glu Leu Tyr Pro Ser Ile Val Glu 55 60 65 cgc gct tcc tac gaa ggg cgt gac agc cta atc gga ttt gat cac tta 355 Arg Ala Ser Tyr Glu Gly Arg Asp Ser Leu Ile Gly Phe Asp His Leu 70 75 80 85 gcc cgg gaa atg gaa aga tta gcc ttc ggc cca cca tcc gaa agt ttt 403 Ala Arg Glu Met Glu Arg Leu Ala Phe Gly Pro Pro Ser Glu Ser Phe 90 95 100 gaa tac ctc caa gaa ctc gta aaa tcc gga gtg gta gac atc act cac 451 Glu Tyr Leu Gln Glu Leu Val Lys Ser Gly Val Val Asp Ile Thr His 105 110 115 ctg cat cgt ggc cgg gaa cca ctg aca gat tta gtt cgt gaa ctt gaa 499 Leu His Arg Gly Arg Glu Pro Leu Thr Asp Leu Val Arg Glu Leu Glu 120 125 130 ata act gtg gtg ata gac gct gtt ctt ccc ccg ccg gga gta gtg cca 547 Ile Thr Val Val Ile Asp Ala Val Leu Pro Pro Pro Gly Val Val Pro 135 140 145 ggc aca ttg gtg cac aat ttg gta aaa gag gga tat gcc aga atg cgt 595 Gly Thr Leu Val His Asn Leu Val Lys Glu Gly Tyr Ala Arg Met Arg 150 155 160 165 cct ggg act cgg ggg tta gat gta gcg gct gac ggc acc gtt caa ggg 643 Pro Gly Thr Arg Gly Leu Asp Val Ala Ala Asp Gly Thr Val Gln Gly 170 175 180 caa cga cat ttg gct gca gtc gga cgg atg acg gaa gat gtg gtt ttg 691 Gln Arg His Leu Ala Ala Val Gly Arg Met Thr Glu Asp Val Val Leu 185 190 195 ggt aat gac aca ttg tcg cga tca tta cat gac ata atc ccg aag tgg 739 Gly Asn Asp Thr Leu Ser Arg Ser Leu His Asp Ile Ile Pro Lys Trp 200 205 210 gct cgt cga gtt atc cgc gac gcg agc acg tat ccc gat agg gta cat 787 Ala Arg Arg Val Ile Arg Asp Ala Ser Thr Tyr Pro Asp Arg Val His 215 220 225 ggt act cca ccg ctt ccg gca cgg ttg gaa ccc tgg gcg gaa aag ctc 835 Gly Thr Pro Pro Leu Pro Ala Arg Leu Glu Pro Trp Ala Glu Lys Leu 230 235 240 245 act tca gat ccg gcc aca tgc cgc cac ctg att gaa gaa ttc ggg agt 883 Thr Ser Asp Pro Ala Thr Cys Arg His Leu Ile Glu Glu Phe Gly Ser 250 255 260 cct gtg aat gta ctc cat tca ggt tct atg cct cgt aat ata aat gag 931 Pro Val Asn Val Leu His Ser Gly Ser Met Pro Arg Asn Ile Asn Glu 265 270 275 ttg gtt gac gcc ggc att cag atg ggg gtg gat act cga ata ttt ttt 979 Leu Val Asp Ala Gly Ile Gln Met Gly Val Asp Thr Arg Ile Phe Phe 280 285 290 gcc cgc aaa gcg aat aag ggt ctt acc ttc gtt gat gcc gtt aaa gac 1027 Ala Arg Lys Ala Asn Lys Gly Leu Thr Phe Val Asp Ala Val Lys Asp 295 300 305 acc ggt cat ggt gta gat gta gcc agt gaa cga gag tta tct cag gtg 1075 Thr Gly His Gly Val Asp Val Ala Ser Glu Arg Glu Leu Ser Gln Val 310 315 320 325 ctt aat cgt gga gtc cca gga gag cgg atc att cta tcc gca gct atc 1123 Leu Asn Arg Gly Val Pro Gly Glu Arg Ile Ile Leu Ser Ala Ala Ile 330 335 340 aaa ccg gac aga cta ttg gca tta gcg atc gaa aat ggc gtg atc atc 1171 Lys Pro Asp Arg Leu Leu Ala Leu Ala Ile Glu Asn Gly Val Ile Ile 345 350 355 tct gtg gat tcg cgt gat gaa tta gat cgc att tcg gct ttg gtt ggt 1219 Ser Val Asp Ser Arg Asp Glu Leu Asp Arg Ile Ser Ala Leu Val Gly 360 365 370 gac cgc gtt gca cga gtt gcg cct aga gta gct cca gat cct gca gtc 1267 Asp Arg Val Ala Arg Val Ala Pro Arg Val Ala Pro Asp Pro Ala Val 375 380 385 tta cct cca act aga ttt ggt gag cgt gct gca gac tgg ggt aat cgg 1315 Leu Pro Pro Thr Arg Phe Gly Glu Arg Ala Ala Asp Trp Gly Asn Arg 390 395 400 405 ctt acc gag gtg ata ccc ggc gtg gat att gtg ggt ctt cac gtt cac 1363 Leu Thr Glu Val Ile Pro Gly Val Asp Ile Val Gly Leu His Val His 410 415 420 ctc cat ggc tat gct gca aaa gac cgt gct ctg gct ctg cag gaa tgt 1411 Leu His Gly Tyr Ala Ala Lys Asp Arg Ala Leu Ala Leu Gln Glu Cys 425 430 435 tgc caa ctc gtc gat tct ctc aga gaa tgc ggg cat tcc cca cag ttt 1459 Cys Gln Leu Val Asp Ser Leu Arg Glu Cys Gly His Ser Pro Gln Phe 440 445 450 att gac ctt gga gga ggg gtg cct atg agc tac att gaa tct gag gaa 1507 Ile Asp Leu Gly Gly Gly Val Pro Met Ser Tyr Ile Glu Ser Glu Glu 455 460 465 gat tgg atc cgt tat caa tcc gct aaa tct gcg act tca gcc ggg tat 1555 Asp Trp Ile Arg Tyr Gln Ser Ala Lys Ser Ala Thr Ser Ala Gly Tyr 470 475 480 485 gcc gaa tcc ttt acg tgg aaa gac gat ccg tta tct aat acg tac ccg 1603 Ala Glu Ser Phe Thr Trp Lys Asp Asp Pro Leu Ser Asn Thr Tyr Pro 490 495 500 ttc tat cag acc cca gtg cgc ggt aat tgg ttg aaa gac gtg ctt tct 1651 Phe Tyr Gln Thr Pro Val Arg Gly Asn Trp Leu Lys Asp Val Leu Ser 505 510 515 aag ggg gta gct cag atg ctc att gac cgg gga ttg cgg tta cac ata 1699 Lys Gly Val Ala Gln Met Leu Ile Asp Arg Gly Leu Arg Leu His Ile 520 525 530 gag cct ggt cga agt tta cta gat ggg tgt ggc gtc act ctt gcc gaa 1747 Glu Pro Gly Arg Ser Leu Leu Asp Gly Cys Gly Val Thr Leu Ala Glu 535 540 545 gtt gct ttt gtg aaa acc cga agt gac ggg ttg cct cta gtg gga ctg 1795 Val Ala Phe Val Lys Thr Arg Ser Asp Gly Leu Pro Leu Val Gly Leu 550 555 560 565 gct atg aac cga acg cag tgc cgg act aca tcc gat gat ttt ctc att 1843 Ala Met Asn Arg Thr Gln Cys Arg Thr Thr Ser Asp Asp Phe Leu Ile 570 575 580 gat ccc ctg cat atc act gac ggt gat gta ggc gag gaa atc gaa gca 1891 Asp Pro Leu His Ile Thr Asp Gly Asp Val Gly Glu Glu Ile Glu Ala 585 590 595 tat cta gtg ggt gcc tac tgc atc gaa gat gag ctg att tta cgc cgg 1939 Tyr Leu Val Gly Ala Tyr Cys Ile Glu Asp Glu Leu Ile Leu Arg Arg 600 605 610 cga atc cgc ttc ccg aga gga gtc aaa cca gga gat atc atc gga att 1987 Arg Ile Arg Phe Pro Arg Gly Val Lys Pro Gly Asp Ile Ile Gly Ile 615 620 625 cct aac acc gca gga tac ttc atg cat atc ttg gaa agt gca tcg cac 2035 Pro Asn Thr Ala Gly Tyr Phe Met His Ile Leu Glu Ser Ala Ser His 630 635 640 645 caa atc ccg ttg gcg aaa aat gta gtg tgg ccg gag ggg cag tta gac 2083 Gln Ile Pro Leu Ala Lys Asn Val Val Trp Pro Glu Gly Gln Leu Asp 650 655 660 gat atc gat gcg gat taagacataa ccattcgcta atc 2121 Asp Ile Asp Ala Asp 665 46 666 PRT Corynebacterium glutamicum 46 Met Ile Pro Lys Pro Asp Val Thr Asp Leu Tyr Leu Glu Asp Leu Leu 1 5 10 15 Asn Glu Gly Ser Glu Lys Ile Arg Ser Ala Lys Asp Leu Ser Glu Leu 20 25 30 Arg Thr Val Leu Lys Glu Val Ser Ser Gln Ile Gln Glu Arg Ala Gly 35 40 45 Lys Lys Asp Glu Glu Trp Gly Met Gly Ala Thr Trp Arg Glu Leu Tyr 50 55 60 Pro Ser Ile Val Glu Arg Ala Ser Tyr Glu Gly Arg Asp Ser Leu Ile 65 70 75 80 Gly Phe Asp His Leu Ala Arg Glu Met Glu Arg Leu Ala Phe Gly Pro 85 90 95 Pro Ser Glu Ser Phe Glu Tyr Leu Gln Glu Leu Val Lys Ser Gly Val 100 105 110 Val Asp Ile Thr His Leu His Arg Gly Arg Glu Pro Leu Thr Asp Leu 115 120 125 Val Arg Glu Leu Glu Ile Thr Val Val Ile Asp Ala Val Leu Pro Pro 130 135 140 Pro Gly Val Val Pro Gly Thr Leu Val His Asn Leu Val Lys Glu Gly 145 150 155 160 Tyr Ala Arg Met Arg Pro Gly Thr Arg Gly Leu Asp Val Ala Ala Asp 165 170 175 Gly Thr Val Gln Gly Gln Arg His Leu Ala Ala Val Gly Arg Met Thr 180 185 190 Glu Asp Val Val Leu Gly Asn Asp Thr Leu Ser Arg Ser Leu His Asp 195 200 205 Ile Ile Pro Lys Trp Ala Arg Arg Val Ile Arg Asp Ala Ser Thr Tyr 210 215 220 Pro Asp Arg Val His Gly Thr Pro Pro Leu Pro Ala Arg Leu Glu Pro 225 230 235 240 Trp Ala Glu Lys Leu Thr Ser Asp Pro Ala Thr Cys Arg His Leu Ile 245 250 255 Glu Glu Phe Gly Ser Pro Val Asn Val Leu His Ser Gly Ser Met Pro 260 265 270 Arg Asn Ile Asn Glu Leu Val Asp Ala Gly Ile Gln Met Gly Val Asp 275 280 285 Thr Arg Ile Phe Phe Ala Arg Lys Ala Asn Lys Gly Leu Thr Phe Val 290 295 300 Asp Ala Val Lys Asp Thr Gly His Gly Val Asp Val Ala Ser Glu Arg 305 310 315 320 Glu Leu Ser Gln Val Leu Asn Arg Gly Val Pro Gly Glu Arg Ile Ile 325 330 335 Leu Ser Ala Ala Ile Lys Pro Asp Arg Leu Leu Ala Leu Ala Ile Glu 340 345 350 Asn Gly Val Ile Ile Ser Val Asp Ser Arg Asp Glu Leu Asp Arg Ile 355 360 365 Ser Ala Leu Val Gly Asp Arg Val Ala Arg Val Ala Pro Arg Val Ala 370 375 380 Pro Asp Pro Ala Val Leu Pro Pro Thr Arg Phe Gly Glu Arg Ala Ala 385 390 395 400 Asp Trp Gly Asn Arg Leu Thr Glu Val Ile Pro Gly Val Asp Ile Val 405 410 415 Gly Leu His Val His Leu His Gly Tyr Ala Ala Lys Asp Arg Ala Leu 420 425 430 Ala Leu Gln Glu Cys Cys Gln Leu Val Asp Ser Leu Arg Glu Cys Gly 435 440 445 His Ser Pro Gln Phe Ile Asp Leu Gly Gly Gly Val Pro Met Ser Tyr 450 455 460 Ile Glu Ser Glu Glu Asp Trp Ile Arg Tyr Gln Ser Ala Lys Ser Ala 465 470 475 480 Thr Ser Ala Gly Tyr Ala Glu Ser Phe Thr Trp Lys Asp Asp Pro Leu 485 490 495 Ser Asn Thr Tyr Pro Phe Tyr Gln Thr Pro Val Arg Gly Asn Trp Leu 500 505 510 Lys Asp Val Leu Ser Lys Gly Val Ala Gln Met Leu Ile Asp Arg Gly 515 520 525 Leu Arg Leu His Ile Glu Pro Gly Arg Ser Leu Leu Asp Gly Cys Gly 530 535 540 Val Thr Leu Ala Glu Val Ala Phe Val Lys Thr Arg Ser Asp Gly Leu 545 550 555 560 Pro Leu Val Gly Leu Ala Met Asn Arg Thr Gln Cys Arg Thr Thr Ser 565 570 575 Asp Asp Phe Leu Ile Asp Pro Leu His Ile Thr Asp Gly Asp Val Gly 580 585 590 Glu Glu Ile Glu Ala Tyr Leu Val Gly Ala Tyr Cys Ile Glu Asp Glu 595 600 605 Leu Ile Leu Arg Arg Arg Ile Arg Phe Pro Arg Gly Val Lys Pro Gly 610 615 620 Asp Ile Ile Gly Ile Pro Asn Thr Ala Gly Tyr Phe Met His Ile Leu 625 630 635 640 Glu Ser Ala Ser His Gln Ile Pro Leu Ala Lys Asn Val Val Trp Pro 645 650 655 Glu Gly Gln Leu Asp Asp Ile Asp Ala Asp 660 665 47 993 DNA Corynebacterium glutamicum CDS (101)..(970) RXA01393 47 caaaagcaga cctgtaatga agatttccat gatcaccatc gtgacctatg gaagtactta 60 agtaaaatga ttggttctta acatggttta atatagcttc atg aac ccc att caa 115 Met Asn Pro Ile Gln 1 5 ctg gac act ttg ctc tca atc att gat gaa ggc agc ttc gaa ggc gcc 163 Leu Asp Thr Leu Leu Ser Ile Ile Asp Glu Gly Ser Phe Glu Gly Ala 10 15 20 tcc tta gcc ctt tcc att tcc ccc tcg gcg gtg agt cag cgc gtt aaa 211 Ser Leu Ala Leu Ser Ile Ser Pro Ser Ala Val Ser Gln Arg Val Lys 25 30 35 gct ctc gag cat cac gtg ggt cga gtg ttg gta tcg cgc acc caa ccg 259 Ala Leu Glu His His Val Gly Arg Val Leu Val Ser Arg Thr Gln Pro 40 45 50 gcc aaa gca acc gaa gcg ggt gaa gtc ctt gtg caa gca gcg cgg aaa 307 Ala Lys Ala Thr Glu Ala Gly Glu Val Leu Val Gln Ala Ala Arg Lys 55 60 65 atg gtg ttg ctg caa gca gaa act aaa gcg caa cta tct gga cgc ctt 355 Met Val Leu Leu Gln Ala Glu Thr Lys Ala Gln Leu Ser Gly Arg Leu 70 75 80 85 gct gaa atc ccg tta acc atc gcc atc aac gca gat tcg cta tcc aca 403 Ala Glu Ile Pro Leu Thr Ile Ala Ile Asn Ala Asp Ser Leu Ser Thr 90 95 100 tgg ttt cct ccc gtg ttc aac gag gta gct tct tgg ggt gga gca acg 451 Trp Phe Pro Pro Val Phe Asn Glu Val Ala Ser Trp Gly Gly Ala Thr 105 110 115 ctc acg ctg cgc ttg gaa gat gaa gcg cac aca tta tcc ttg ctg cgg 499 Leu Thr Leu Arg Leu Glu Asp Glu Ala His Thr Leu Ser Leu Leu Arg 120 125 130 cgt gga gat gtt tta gga gcg gta acc cgt gaa gct aat ccc gtg gcg 547 Arg Gly Asp Val Leu Gly Ala Val Thr Arg Glu Ala Asn Pro Val Ala 135 140 145 gga tgt gaa gta gta gaa ctt gga acc atg cgc cac ttg gcc att gca 595 Gly Cys Glu Val Val Glu Leu Gly Thr Met Arg His Leu Ala Ile Ala 150 155 160 165 acc ccc tca ttg cgg gat gcc tac atg gtt gat ggg aaa cta gat tgg 643 Thr Pro Ser Leu Arg Asp Ala Tyr Met Val Asp Gly Lys Leu Asp Trp 170 175 180 gct gcg atg ccc gtc tta cgc ttc ggt ccc aaa gat gtg ctt caa gac 691 Ala Ala Met Pro Val Leu Arg Phe Gly Pro Lys Asp Val Leu Gln Asp 185 190 195 cgt gac ctg gac ggg cgc gtc gat ggt cct gtg ggg cgc agg cgc gta 739 Arg Asp Leu Asp Gly Arg Val Asp Gly Pro Val Gly Arg Arg Arg Val 200 205 210 tcc att gtc ccg tcg gcg gaa ggt ttt ggt gag gca att cgc cga ggc 787 Ser Ile Val Pro Ser Ala Glu Gly Phe Gly Glu Ala Ile Arg Arg Gly 215 220 225 ctt ggt tgg gga ctt ctt ccc gaa acc caa gct gct ccc atg cta aaa 835 Leu Gly Trp Gly Leu Leu Pro Glu Thr Gln Ala Ala Pro Met Leu Lys 230 235 240 245 gca gga gaa gtg atc ctc ctc gat gag ata ccc att gac aca ccg atg 883 Ala Gly Glu Val Ile Leu Leu Asp Glu Ile Pro Ile Asp Thr Pro Met 250 255 260 tat tgg caa cga tgg cgc ctg gaa tct aga tct cta gct aga ctc aca 931 Tyr Trp Gln Arg Trp Arg Leu Glu Ser Arg Ser Leu Ala Arg Leu Thr 265 270 275 gac gcc gtc gtt gat gca gca atc gag gga ttg cgg cct tagttacttc 980 Asp Ala Val Val Asp Ala Ala Ile Glu Gly Leu Arg Pro 280 285 290 tgaaaaggtt cag 993 48 290 PRT Corynebacterium glutamicum 48 Met Asn Pro Ile Gln Leu Asp Thr Leu Leu Ser Ile Ile Asp Glu Gly 1 5 10 15 Ser Phe Glu Gly Ala Ser Leu Ala Leu Ser Ile Ser Pro Ser Ala Val 20 25 30 Ser Gln Arg Val Lys Ala Leu Glu His His Val Gly Arg Val Leu Val 35 40 45 Ser Arg Thr Gln Pro Ala Lys Ala Thr Glu Ala Gly Glu Val Leu Val 50 55 60 Gln Ala Ala Arg Lys Met Val Leu Leu Gln Ala Glu Thr Lys Ala Gln 65 70 75 80 Leu Ser Gly Arg Leu Ala Glu Ile Pro Leu Thr Ile Ala Ile Asn Ala 85 90 95 Asp Ser Leu Ser Thr Trp Phe Pro Pro Val Phe Asn Glu Val Ala Ser 100 105 110 Trp Gly Gly Ala Thr Leu Thr Leu Arg Leu Glu Asp Glu Ala His Thr 115 120 125 Leu Ser Leu Leu Arg Arg Gly Asp Val Leu Gly Ala Val Thr Arg Glu 130 135 140 Ala Asn Pro Val Ala Gly Cys Glu Val Val Glu Leu Gly Thr Met Arg 145 150 155 160 His Leu Ala Ile Ala Thr Pro Ser Leu Arg Asp Ala Tyr Met Val Asp 165 170 175 Gly Lys Leu Asp Trp Ala Ala Met Pro Val Leu Arg Phe Gly Pro Lys 180 185 190 Asp Val Leu Gln Asp Arg Asp Leu Asp Gly Arg Val Asp Gly Pro Val 195 200 205 Gly Arg Arg Arg Val Ser Ile Val Pro Ser Ala Glu Gly Phe Gly Glu 210 215 220 Ala Ile Arg Arg Gly Leu Gly Trp Gly Leu Leu Pro Glu Thr Gln Ala 225 230 235 240 Ala Pro Met Leu Lys Ala Gly Glu Val Ile Leu Leu Asp Glu Ile Pro 245 250 255 Ile Asp Thr Pro Met Tyr Trp Gln Arg Trp Arg Leu Glu Ser Arg Ser 260 265 270 Leu Ala Arg Leu Thr Asp Ala Val Val Asp Ala Ala Ile Glu Gly Leu 275 280 285 Arg Pro 290 49 1626 DNA Corynebacterium glutamicum CDS (101)..(1603) RXA00241 49 ggtctccagc ctttctaaac aattcatctg cacttgatta attggcccca agattacgcg 60 aagtttagcg acttcgccgt acgtcaacta cgttaaatga gtg aat act caa tca 115 Val Asn Thr Gln Ser 1 5 gat tct gcg ggg tct caa ggt gca gcg gcc aca agt cgt act gta tct 163 Asp Ser Ala Gly Ser Gln Gly Ala Ala Ala Thr Ser Arg Thr Val Ser 10 15 20 att aga acc ctc atc gcg ctg atc atc gga tcg acc gtc ggc gcg gga 211 Ile Arg Thr Leu Ile Ala Leu Ile Ile Gly Ser Thr Val Gly Ala Gly 25 30 35 att ttc tcc atc cct caa aac atc ggc tca gtc gca ggt ccc ggc gcg 259 Ile Phe Ser Ile Pro Gln Asn Ile Gly Ser Val Ala Gly Pro Gly Ala 40 45 50 atg ctc atc ggc tgg ctg atc gcc ggt gtg ggc atg ttg tcc gta gcg 307 Met Leu Ile Gly Trp Leu Ile Ala Gly Val Gly Met Leu Ser Val Ala 55 60 65 ttc gtg ttc cat gtt ctt gcc cgc cgt aaa cct cac ctc gat tct ggc 355 Phe Val Phe His Val Leu Ala Arg Arg Lys Pro His Leu Asp Ser Gly 70 75 80 85 gtc tac gca tat gcg cgt gtt gga ttg ggc gat tat gta ggt ttc tcc 403 Val Tyr Ala Tyr Ala Arg Val Gly Leu Gly Asp Tyr Val Gly Phe Ser 90 95 100 tcc gct tgg ggt tat tgg ctg ggt tca gtc atc gcc caa gtt ggc tac 451 Ser Ala Trp Gly Tyr Trp Leu Gly Ser Val Ile Ala Gln Val Gly Tyr 105 110 115 gca acg tta ttt ttc tcc acg ttg ggc cac tac gta ccg ctg ttt tcc 499 Ala Thr Leu Phe Phe Ser Thr Leu Gly His Tyr Val Pro Leu Phe Ser 120 125 130 caa gat cat cca ttt gtg tca gcg ttg gca gtt agc gct ttg acc tgg 547 Gln Asp His Pro Phe Val Ser Ala Leu Ala Val Ser Ala Leu Thr Trp 135 140 145 ctg gtg ttt gga gtt gtt tcc cga gga att agc caa gct gct ttc ttg 595 Leu Val Phe Gly Val Val Ser Arg Gly Ile Ser Gln Ala Ala Phe Leu 150 155 160 165 aca acg gtc acc acc gtg gcc aaa att ctg cct ctg ttg tgc ttc atc 643 Thr Thr Val Thr Thr Val Ala Lys Ile Leu Pro Leu Leu Cys Phe Ile 170 175 180 atc ctt gtt gca ttc ttg ggc ttt agc tgg gag aag ttc act gtt gat 691 Ile Leu Val Ala Phe Leu Gly Phe Ser Trp Glu Lys Phe Thr Val Asp 185 190 195 tta tgg gcg cgt gat ggt ggc gtg ggc agc att ttt gat cag gtg cgc 739 Leu Trp Ala Arg Asp Gly Gly Val Gly Ser Ile Phe Asp Gln Val Arg 200 205 210 ggc atc atg gtg tac acc gtg tgg gtg ttc atc ggt atc gaa ggt gca 787 Gly Ile Met Val Tyr Thr Val Trp Val Phe Ile Gly Ile Glu Gly Ala 215 220 225 tcg gta tat tcc cgc cag gca cgc tca cgc agt gat gtc agc cga gct 835 Ser Val Tyr Ser Arg Gln Ala Arg Ser Arg Ser Asp Val Ser Arg Ala 230 235 240 245 acc gtg att ggt ttt gtg gct gtt ctc ctt ttg ctg gtg tcg att tct 883 Thr Val Ile Gly Phe Val Ala Val Leu Leu Leu Leu Val Ser Ile Ser 250 255 260 tcg ctg agc ttc ggt gta ctg acc caa caa gag ctc gct gcg tta cca 931 Ser Leu Ser Phe Gly Val Leu Thr Gln Gln Glu Leu Ala Ala Leu Pro 265 270 275 gat aat tcc atg gcg tcg gtg ctc gaa gct gtt gtt ggt cca tgg ggt 979 Asp Asn Ser Met Ala Ser Val Leu Glu Ala Val Val Gly Pro Trp Gly 280 285 290 gcc gca ttg att tcg ttg ggt ctg tgt ctt tcg gtt ctt ggg gcc tat 1027 Ala Ala Leu Ile Ser Leu Gly Leu Cys Leu Ser Val Leu Gly Ala Tyr 295 300 305 gtg tcc tgg cag atg ctc tgc gca gaa cca ctg gcg ttg atg gca atg 1075 Val Ser Trp Gln Met Leu Cys Ala Glu Pro Leu Ala Leu Met Ala Met 310 315 320 325 gat ggc ctc att cca agc aaa atc ggg gcc atc aac agc cgc ggt gct 1123 Asp Gly Leu Ile Pro Ser Lys Ile Gly Ala Ile Asn Ser Arg Gly Ala 330 335 340 gcc tgg atg gct cag ctg atc tcc acc atc gtg att cag att ttc atc 1171 Ala Trp Met Ala Gln Leu Ile Ser Thr Ile Val Ile Gln Ile Phe Ile 345 350 355 atc att ttc ttc ctc aac gag acc acc tac gtc tcc atg gtg caa ttg 1219 Ile Ile Phe Phe Leu Asn Glu Thr Thr Tyr Val Ser Met Val Gln Leu 360 365 370 gct acc aac cta tac ttg gtg cct tac ctg ttc tct gcc ttt tat ctg 1267 Ala Thr Asn Leu Tyr Leu Val Pro Tyr Leu Phe Ser Ala Phe Tyr Leu 375 380 385 gtc atg ctg gca aca cgt gga aaa gga atc acc cac cca cat gcc ggc 1315 Val Met Leu Ala Thr Arg Gly Lys Gly Ile Thr His Pro His Ala Gly 390 395 400 405 aca cgt ttt gat gat tcc ggt cca gag ata tcc cgc cga gaa aac cgc 1363 Thr Arg Phe Asp Asp Ser Gly Pro Glu Ile Ser Arg Arg Glu Asn Arg 410 415 420 aaa cac ctc atc gtc ggt tta gta gca acg gtg tat tca gtg tgg ctg 1411 Lys His Leu Ile Val Gly Leu Val Ala Thr Val Tyr Ser Val Trp Leu 425 430 435 ttt tac gct gca gaa ccg cag ttt gtc ctc ttc gga gcc atg gcg atg 1459 Phe Tyr Ala Ala Glu Pro Gln Phe Val Leu Phe Gly Ala Met Ala Met 440 445 450 ctt ccc ggc tta atc ccc tat gtg tgg aca agg att tat cgt ggc gaa 1507 Leu Pro Gly Leu Ile Pro Tyr Val Trp Thr Arg Ile Tyr Arg Gly Glu 455 460 465 cag gtg ttt aac cgc ttt gaa atc ggc gtg gtt gtt gtc ctg gtc gtt 1555 Gln Val Phe Asn Arg Phe Glu Ile Gly Val Val Val Val Leu Val Val 470 475 480 485 gct gcc agc gcg ggc gtt att ggt ttg gtc aac gga tca cta tcg ctt 1603 Ala Ala Ser Ala Gly Val Ile Gly Leu Val Asn Gly Ser Leu Ser Leu 490 495 500 taaacaccga aaccttcctg cta 1626 50 501 PRT Corynebacterium glutamicum 50 Val Asn Thr Gln Ser Asp Ser Ala Gly Ser Gln Gly Ala Ala Ala Thr 1 5 10 15 Ser Arg Thr Val Ser Ile Arg Thr Leu Ile Ala Leu Ile Ile Gly Ser 20 25 30 Thr Val Gly Ala Gly Ile Phe Ser Ile Pro Gln Asn Ile Gly Ser Val 35 40 45 Ala Gly Pro Gly Ala Met Leu Ile Gly Trp Leu Ile Ala Gly Val Gly 50 55 60 Met Leu Ser Val Ala Phe Val Phe His Val Leu Ala Arg Arg Lys Pro 65 70 75 80 His Leu Asp Ser Gly Val Tyr Ala Tyr Ala Arg Val Gly Leu Gly Asp 85 90 95 Tyr Val Gly Phe Ser Ser Ala Trp Gly Tyr Trp Leu Gly Ser Val Ile 100 105 110 Ala Gln Val Gly Tyr Ala Thr Leu Phe Phe Ser Thr Leu Gly His Tyr 115 120 125 Val Pro Leu Phe Ser Gln Asp His Pro Phe Val Ser Ala Leu Ala Val 130 135 140 Ser Ala Leu Thr Trp Leu Val Phe Gly Val Val Ser Arg Gly Ile Ser 145 150 155 160 Gln Ala Ala Phe Leu Thr Thr Val Thr Thr Val Ala Lys Ile Leu Pro 165 170 175 Leu Leu Cys Phe Ile Ile Leu Val Ala Phe Leu Gly Phe Ser Trp Glu 180 185 190 Lys Phe Thr Val Asp Leu Trp Ala Arg Asp Gly Gly Val Gly Ser Ile 195 200 205 Phe Asp Gln Val Arg Gly Ile Met Val Tyr Thr Val Trp Val Phe Ile 210 215 220 Gly Ile Glu Gly Ala Ser Val Tyr Ser Arg Gln Ala Arg Ser Arg Ser 225 230 235 240 Asp Val Ser Arg Ala Thr Val Ile Gly Phe Val Ala Val Leu Leu Leu 245 250 255 Leu Val Ser Ile Ser Ser Leu Ser Phe Gly Val Leu Thr Gln Gln Glu 260 265 270 Leu Ala Ala Leu Pro Asp Asn Ser Met Ala Ser Val Leu Glu Ala Val 275 280 285 Val Gly Pro Trp Gly Ala Ala Leu Ile Ser Leu Gly Leu Cys Leu Ser 290 295 300 Val Leu Gly Ala Tyr Val Ser Trp Gln Met Leu Cys Ala Glu Pro Leu 305 310 315 320 Ala Leu Met Ala Met Asp Gly Leu Ile Pro Ser Lys Ile Gly Ala Ile 325 330 335 Asn Ser Arg Gly Ala Ala Trp Met Ala Gln Leu Ile Ser Thr Ile Val 340 345 350 Ile Gln Ile Phe Ile Ile Ile Phe Phe Leu Asn Glu Thr Thr Tyr Val 355 360 365 Ser Met Val Gln Leu Ala Thr Asn Leu Tyr Leu Val Pro Tyr Leu Phe 370 375 380 Ser Ala Phe Tyr Leu Val Met Leu Ala Thr Arg Gly Lys Gly Ile Thr 385 390 395 400 His Pro His Ala Gly Thr Arg Phe Asp Asp Ser Gly Pro Glu Ile Ser 405 410 415 Arg Arg Glu Asn Arg Lys His Leu Ile Val Gly Leu Val Ala Thr Val 420 425 430 Tyr Ser Val Trp Leu Phe Tyr Ala Ala Glu Pro Gln Phe Val Leu Phe 435 440 445 Gly Ala Met Ala Met Leu Pro Gly Leu Ile Pro Tyr Val Trp Thr Arg 450 455 460 Ile Tyr Arg Gly Glu Gln Val Phe Asn Arg Phe Glu Ile Gly Val Val 465 470 475 480 Val Val Leu Val Val Ala Ala Ser Ala Gly Val Ile Gly Leu Val Asn 485 490 495 Gly Ser Leu Ser Leu 500 51 822 DNA Corynebacterium glutamicum CDS (101)..(799) RXA01394 51 gagcaaagtg tccagttgaa tggggttcat gaagctatat taaaccatgt taagaaccaa 60 tcattttact taagtacttc cataggtcac gatggtgatc atg gaa atc ttc att 115 Met Glu Ile Phe Ile 1 5 aca ggt ctg ctt ttg ggg gcc agt ctt tta ctg tcc atc gga ccg cag 163 Thr Gly Leu Leu Leu Gly Ala Ser Leu Leu Leu Ser Ile Gly Pro Gln 10 15 20 aat gta ctg gtg att aaa caa gga att aag cgc gaa gga ctc att gcg 211 Asn Val Leu Val Ile Lys Gln Gly Ile Lys Arg Glu Gly Leu Ile Ala 25 30 35 gtt ctt ctc gtg tgt tta att tct gac gtc ttt ttg ttc atc gcc ggc 259 Val Leu Leu Val Cys Leu Ile Ser Asp Val Phe Leu Phe Ile Ala Gly 40 45 50 acc ttg ggc gtt gat ctt ttg tcc aat gcc gcg ccg atc gtg ctc gat 307 Thr Leu Gly Val Asp Leu Leu Ser Asn Ala Ala Pro Ile Val Leu Asp 55 60 65 att atg cgc tgg ggt ggc atc gct tac ctg tta tgg ttt gcc gtc atg 355 Ile Met Arg Trp Gly Gly Ile Ala Tyr Leu Leu Trp Phe Ala Val Met 70 75 80 85 gca gcg aaa gac gcc atg aca aac aag gtg gaa gcg cca cag atc att 403 Ala Ala Lys Asp Ala Met Thr Asn Lys Val Glu Ala Pro Gln Ile Ile 90 95 100 gaa gaa aca gaa cca acc gtg ccc gat gac acg cct ttg ggc ggt tcg 451 Glu Glu Thr Glu Pro Thr Val Pro Asp Asp Thr Pro Leu Gly Gly Ser 105 110 115 gcg gtg gcc act gac acg cgc aac cgg gtg cgg gtg gag gtg agc gtc 499 Ala Val Ala Thr Asp Thr Arg Asn Arg Val Arg Val Glu Val Ser Val 120 125 130 gat aag cag cgg gtt tgg gta aag ccc atg ttg atg gca atc gtg ctg 547 Asp Lys Gln Arg Val Trp Val Lys Pro Met Leu Met Ala Ile Val Leu 135 140 145 acc tgg ttg aac ccg aat gcg tat ttg gac gcg ttt gtg ttt atc ggc 595 Thr Trp Leu Asn Pro Asn Ala Tyr Leu Asp Ala Phe Val Phe Ile Gly 150 155 160 165 ggc gtc ggc gcg caa tac ggc gac acc gga cgg tgg att ttc gcc gct 643 Gly Val Gly Ala Gln Tyr Gly Asp Thr Gly Arg Trp Ile Phe Ala Ala 170 175 180 ggc gcg ttc gcg gca agc ctg atc tgg ttc ccg ctg gtg ggt ttc ggc 691 Gly Ala Phe Ala Ala Ser Leu Ile Trp Phe Pro Leu Val Gly Phe Gly 185 190 195 gca gca gca ttg tca cgc ccg ctg tcc agc ccc aag gtg tgg cgc tgg 739 Ala Ala Ala Leu Ser Arg Pro Leu Ser Ser Pro Lys Val Trp Arg Trp 200 205 210 atc aac gtc gtc gtg gca gtt gtg atg acc gca ttg gcc atc aaa ctg 787 Ile Asn Val Val Val Ala Val Val Met Thr Ala Leu Ala Ile Lys Leu 215 220 225 atg ttg atg ggt tagttttcgc gggttttgga atc 822 Met Leu Met Gly 230 52 233 PRT Corynebacterium glutamicum 52 Met Glu Ile Phe Ile Thr Gly Leu Leu Leu Gly Ala Ser Leu Leu Leu 1 5 10 15 Ser Ile Gly Pro Gln Asn Val Leu Val Ile Lys Gln Gly Ile Lys Arg 20 25 30 Glu Gly Leu Ile Ala Val Leu Leu Val Cys Leu Ile Ser Asp Val Phe 35 40 45 Leu Phe Ile Ala Gly Thr Leu Gly Val Asp Leu Leu Ser Asn Ala Ala 50 55 60 Pro Ile Val Leu Asp Ile Met Arg Trp Gly Gly Ile Ala Tyr Leu Leu 65 70 75 80 Trp Phe Ala Val Met Ala Ala Lys Asp Ala Met Thr Asn Lys Val Glu 85 90 95 Ala Pro Gln Ile Ile Glu Glu Thr Glu Pro Thr Val Pro Asp Asp Thr 100 105 110 Pro Leu Gly Gly Ser Ala Val Ala Thr Asp Thr Arg Asn Arg Val Arg 115 120 125 Val Glu Val Ser Val Asp Lys Gln Arg Val Trp Val Lys Pro Met Leu 130 135 140 Met Ala Ile Val Leu Thr Trp Leu Asn Pro Asn Ala Tyr Leu Asp Ala 145 150 155 160 Phe Val Phe Ile Gly Gly Val Gly Ala Gln Tyr Gly Asp Thr Gly Arg 165 170 175 Trp Ile Phe Ala Ala Gly Ala Phe Ala Ala Ser Leu Ile Trp Phe Pro 180 185 190 Leu Val Gly Phe Gly Ala Ala Ala Leu Ser Arg Pro Leu Ser Ser Pro 195 200 205 Lys Val Trp Arg Trp Ile Asn Val Val Val Ala Val Val Met Thr Ala 210 215 220 Leu Ala Ile Lys Leu Met Leu Met Gly 225 230 53 1026 DNA Corynebacterium glutamicum CDS (101)..(1003) RXA00865 53 ttatcggaat gtggcttggg cgattgttat gcaaaagttg ttaggttttt tgcggggttg 60 tttaaccccc aaatgaggga agaaggtaac cttgaactct atg agc aca ggt tta 115 Met Ser Thr Gly Leu 1 5 aca gct aag acc gga gta gag cac ttc ggc acc gtt gga gta gca atg 163 Thr Ala Lys Thr Gly Val Glu His Phe Gly Thr Val Gly Val Ala Met 10 15 20 gtt act cca ttc acg gaa tcc gga gac atc gat atc gct gct ggc cgc 211 Val Thr Pro Phe Thr Glu Ser Gly Asp Ile Asp Ile Ala Ala Gly Arg 25 30 35 gaa gtc gcg gct tat ttg gtt gat aag ggc ttg gat tct ttg gtt ctc 259 Glu Val Ala Ala Tyr Leu Val Asp Lys Gly Leu Asp Ser Leu Val Leu 40 45 50 gcg ggc acc act ggt gaa tcc cca acg aca acc gcc gct gaa aaa cta 307 Ala Gly Thr Thr Gly Glu Ser Pro Thr Thr Thr Ala Ala Glu Lys Leu 55 60 65 gaa ctg ctc aag gcc gtt cgt gag gaa gtt ggg gat cgg gcg aag ctc 355 Glu Leu Leu Lys Ala Val Arg Glu Glu Val Gly Asp Arg Ala Lys Leu 70 75 80 85 atc gcc ggt gtc gga acc aac aac acg cgg aca tct gtg gaa ctt gcg 403 Ile Ala Gly Val Gly Thr Asn Asn Thr Arg Thr Ser Val Glu Leu Ala 90 95 100 gaa gct gct gct tct gct ggc gca gac ggc ctt tta gtt gta act cct 451 Glu Ala Ala Ala Ser Ala Gly Ala Asp Gly Leu Leu Val Val Thr Pro 105 110 115 tat tac tcc aag ccg agc caa gag gga ttg ctg gcg cac ttc ggt gca 499 Tyr Tyr Ser Lys Pro Ser Gln Glu Gly Leu Leu Ala His Phe Gly Ala 120 125 130 att gct gca gca aca gag gtt cca att tgt ctc tat gac att cct ggt 547 Ile Ala Ala Ala Thr Glu Val Pro Ile Cys Leu Tyr Asp Ile Pro Gly 135 140 145 cgg tca ggt att cca att gag tct gat acc atg aga cgc ctg agt gaa 595 Arg Ser Gly Ile Pro Ile Glu Ser Asp Thr Met Arg Arg Leu Ser Glu 150 155 160 165 tta cct acg att ttg gcg gtc aag gac gcc aag ggt gac ctc gtt gca 643 Leu Pro Thr Ile Leu Ala Val Lys Asp Ala Lys Gly Asp Leu Val Ala 170 175 180 gcc acg tca ttg atc aaa gaa acg gga ctt gcc tgg tat tca ggc gat 691 Ala Thr Ser Leu Ile Lys Glu Thr Gly Leu Ala Trp Tyr Ser Gly Asp 185 190 195 gac cca cta aac ctt gtt tgg ctt gct ttg ggc gga tca ggt ttc att 739 Asp Pro Leu Asn Leu Val Trp Leu Ala Leu Gly Gly Ser Gly Phe Ile 200 205 210 tcc gta att gga cat gca gcc ccc aca gca tta cgt gag ttg tac aca 787 Ser Val Ile Gly His Ala Ala Pro Thr Ala Leu Arg Glu Leu Tyr Thr 215 220 225 agc ttc gag gaa ggc gac ctc gtc cgt gcg cgg gaa atc aac gcc aaa 835 Ser Phe Glu Glu Gly Asp Leu Val Arg Ala Arg Glu Ile Asn Ala Lys 230 235 240 245 cta tca ccg ctg gta gct gcc caa ggt cgc ttg ggt gga gtc agc ttg 883 Leu Ser Pro Leu Val Ala Ala Gln Gly Arg Leu Gly Gly Val Ser Leu 250 255 260 gca aaa gct gct ctg cgt ctg cag ggc atc aac gta gga gat cct cga 931 Ala Lys Ala Ala Leu Arg Leu Gln Gly Ile Asn Val Gly Asp Pro Arg 265 270 275 ctt cca att atg gct cca aat gag cag gaa ctt gag gct ctc cga gaa 979 Leu Pro Ile Met Ala Pro Asn Glu Gln Glu Leu Glu Ala Leu Arg Glu 280 285 290 gac atg aaa aaa gct gga gtt cta taaatatgaa tgattcccga aat 1026 Asp Met Lys Lys Ala Gly Val Leu 295 300 54 301 PRT Corynebacterium glutamicum 54 Met Ser Thr Gly Leu Thr Ala Lys Thr Gly Val Glu His Phe Gly Thr 1 5 10 15 Val Gly Val Ala Met Val Thr Pro Phe Thr Glu Ser Gly Asp Ile Asp 20 25 30 Ile Ala Ala Gly Arg Glu Val Ala Ala Tyr Leu Val Asp Lys Gly Leu 35 40 45 Asp Ser Leu Val Leu Ala Gly Thr Thr Gly Glu Ser Pro Thr Thr Thr 50 55 60 Ala Ala Glu Lys Leu Glu Leu Leu Lys Ala Val Arg Glu Glu Val Gly 65 70 75 80 Asp Arg Ala Lys Leu Ile Ala Gly Val Gly Thr Asn Asn Thr Arg Thr 85 90 95 Ser Val Glu Leu Ala Glu Ala Ala Ala Ser Ala Gly Ala Asp Gly Leu 100 105 110 Leu Val Val Thr Pro Tyr Tyr Ser Lys Pro Ser Gln Glu Gly Leu Leu 115 120 125 Ala His Phe Gly Ala Ile Ala Ala Ala Thr Glu Val Pro Ile Cys Leu 130 135 140 Tyr Asp Ile Pro Gly Arg Ser Gly Ile Pro Ile Glu Ser Asp Thr Met 145 150 155 160 Arg Arg Leu Ser Glu Leu Pro Thr Ile Leu Ala Val Lys Asp Ala Lys 165 170 175 Gly Asp Leu Val Ala Ala Thr Ser Leu Ile Lys Glu Thr Gly Leu Ala 180 185 190 Trp Tyr Ser Gly Asp Asp Pro Leu Asn Leu Val Trp Leu Ala Leu Gly 195 200 205 Gly Ser Gly Phe Ile Ser Val Ile Gly His Ala Ala Pro Thr Ala Leu 210 215 220 Arg Glu Leu Tyr Thr Ser Phe Glu Glu Gly Asp Leu Val Arg Ala Arg 225 230 235 240 Glu Ile Asn Ala Lys Leu Ser Pro Leu Val Ala Ala Gln Gly Arg Leu 245 250 255 Gly Gly Val Ser Leu Ala Lys Ala Ala Leu Arg Leu Gln Gly Ile Asn 260 265 270 Val Gly Asp Pro Arg Leu Pro Ile Met Ala Pro Asn Glu Gln Glu Leu 275 280 285 Glu Ala Leu Arg Glu Asp Met Lys Lys Ala Gly Val Leu 290 295 300 55 1071 DNA Corynebacterium glutamicum CDS (101)..(1048) RXS02021 55 ttgggtcgcc gaggagatct aatcctggtt tgagttcaga gttcacaggt ttaagcctac 60 aaaccttagt taaaacatga tggaagcggt cgattaaaaa atg agt gaa aac att 115 Met Ser Glu Asn Ile 1 5 cgc gga gcc caa gca gtt gga atc gca aat atc gcc atg gac ggg acc 163 Arg Gly Ala Gln Ala Val Gly Ile Ala Asn Ile Ala Met Asp Gly Thr 10 15 20 atc ctg gac acg tgg tac cca gaa ccc caa att ttc aac ccg gat cag 211 Ile Leu Asp Thr Trp Tyr Pro Glu Pro Gln Ile Phe Asn Pro Asp Gln 25 30 35 tgg gct gaa cgc tac cca ttg gaa gtg ggc acc aca cgc ctc gga gca 259 Trp Ala Glu Arg Tyr Pro Leu Glu Val Gly Thr Thr Arg Leu Gly Ala 40 45 50 aac gaa ctc acc cca cgg atg ctg cag ttg gta aaa ctg gac caa gat 307 Asn Glu Leu Thr Pro Arg Met Leu Gln Leu Val Lys Leu Asp Gln Asp 55 60 65 cgc ctc gtc gaa cag gta gca gtc cgc acc gtt atc ccc gat ctg tct 355 Arg Leu Val Glu Gln Val Ala Val Arg Thr Val Ile Pro Asp Leu Ser 70 75 80 85 caa cct cca gta gac gcg cac gat gtt tac ctg cgc ctc cac ctg ctt 403 Gln Pro Pro Val Asp Ala His Asp Val Tyr Leu Arg Leu His Leu Leu 90 95 100 tcc cac cgg ctg gtc cgc ccc cac gaa atg cac atg caa aac acc ttg 451 Ser His Arg Leu Val Arg Pro His Glu Met His Met Gln Asn Thr Leu 105 110 115 gag ctg ctg tcc gac gtg gtg tgg aca aac aag ggc cct tgc ctt cct 499 Glu Leu Leu Ser Asp Val Val Trp Thr Asn Lys Gly Pro Cys Leu Pro 120 125 130 gaa aac ttt gag tgg gtg cgt ggt gct ctg cgg tcc cgc gga ctc atc 547 Glu Asn Phe Glu Trp Val Arg Gly Ala Leu Arg Ser Arg Gly Leu Ile 135 140 145 cac gtc tac tgt gtg gac cgt ctt ccc cgc atg gtc gac tat gtg gtt 595 His Val Tyr Cys Val Asp Arg Leu Pro Arg Met Val Asp Tyr Val Val 150 155 160 165 ccc cct gga gtc cgc atc tcc gaa gca gaa cgc gtg cgc cta ggt gca 643 Pro Pro Gly Val Arg Ile Ser Glu Ala Glu Arg Val Arg Leu Gly Ala 170 175 180 tac ctt gct ccg ggt acc tct gtg ctg cgt gaa ggt ttc gtg tct ttc 691 Tyr Leu Ala Pro Gly Thr Ser Val Leu Arg Glu Gly Phe Val Ser Phe 185 190 195 aac tcc ggc acc ttg ggt gcc gca aag gtg gaa ggc cgc ctg agt tcc 739 Asn Ser Gly Thr Leu Gly Ala Ala Lys Val Glu Gly Arg Leu Ser Ser 200 205 210 ggt gtg gtc atc ggt gaa ggt tcc gag att gga ctg tct tct act att 787 Gly Val Val Ile Gly Glu Gly Ser Glu Ile Gly Leu Ser Ser Thr Ile 215 220 225 cag tcc ccg aga gat gaa cag cgc cgc cgt ttg ccg ttg agc atc ggc 835 Gln Ser Pro Arg Asp Glu Gln Arg Arg Arg Leu Pro Leu Ser Ile Gly 230 235 240 245 caa aac tgc aac ttt ggt gtc agc tcc gga atc atc gga gtc agt ctg 883 Gln Asn Cys Asn Phe Gly Val Ser Ser Gly Ile Ile Gly Val Ser Leu 250 255 260 gga gac aat tgc gac atc gga aat aac att gtc ttg gat gga gat acc 931 Gly Asp Asn Cys Asp Ile Gly Asn Asn Ile Val Leu Asp Gly Asp Thr 265 270 275 ccc att tgg ttc gca gcc gat gag gag tta cgc act atc gac tcc atc 979 Pro Ile Trp Phe Ala Ala Asp Glu Glu Leu Arg Thr Ile Asp Ser Ile 280 285 290 gaa ggc caa gca aat tgg tca atc aag cgt gaa tcc ggc ttc cat gag 1027 Glu Gly Gln Ala Asn Trp Ser Ile Lys Arg Glu Ser Gly Phe His Glu 295 300 305 cca gtt gcc cgc ctc aaa gct tgacccattt tcataaccag tgc 1071 Pro Val Ala Arg Leu Lys Ala 310 315 56 316 PRT Corynebacterium glutamicum 56 Met Ser Glu Asn Ile Arg Gly Ala Gln Ala Val Gly Ile Ala Asn Ile 1 5 10 15 Ala Met Asp Gly Thr Ile Leu Asp Thr Trp Tyr Pro Glu Pro Gln Ile 20 25 30 Phe Asn Pro Asp Gln Trp Ala Glu Arg Tyr Pro Leu Glu Val Gly Thr 35 40 45 Thr Arg Leu Gly Ala Asn Glu Leu Thr Pro Arg Met Leu Gln Leu Val 50 55 60 Lys Leu Asp Gln Asp Arg Leu Val Glu Gln Val Ala Val Arg Thr Val 65 70 75 80 Ile Pro Asp Leu Ser Gln Pro Pro Val Asp Ala His Asp Val Tyr Leu 85 90 95 Arg Leu His Leu Leu Ser His Arg Leu Val Arg Pro His Glu Met His 100 105 110 Met Gln Asn Thr Leu Glu Leu Leu Ser Asp Val Val Trp Thr Asn Lys 115 120 125 Gly Pro Cys Leu Pro Glu Asn Phe Glu Trp Val Arg Gly Ala Leu Arg 130 135 140 Ser Arg Gly Leu Ile His Val Tyr Cys Val Asp Arg Leu Pro Arg Met 145 150 155 160 Val Asp Tyr Val Val Pro Pro Gly Val Arg Ile Ser Glu Ala Glu Arg 165 170 175 Val Arg Leu Gly Ala Tyr Leu Ala Pro Gly Thr Ser Val Leu Arg Glu 180 185 190 Gly Phe Val Ser Phe Asn Ser Gly Thr Leu Gly Ala Ala Lys Val Glu 195 200 205 Gly Arg Leu Ser Ser Gly Val Val Ile Gly Glu Gly Ser Glu Ile Gly 210 215 220 Leu Ser Ser Thr Ile Gln Ser Pro Arg Asp Glu Gln Arg Arg Arg Leu 225 230 235 240 Pro Leu Ser Ile Gly Gln Asn Cys Asn Phe Gly Val Ser Ser Gly Ile 245 250 255 Ile Gly Val Ser Leu Gly Asp Asn Cys Asp Ile Gly Asn Asn Ile Val 260 265 270 Leu Asp Gly Asp Thr Pro Ile Trp Phe Ala Ala Asp Glu Glu Leu Arg 275 280 285 Thr Ile Asp Ser Ile Glu Gly Gln Ala Asn Trp Ser Ile Lys Arg Glu 290 295 300 Ser Gly Phe His Glu Pro Val Ala Arg Leu Lys Ala 305 310 315 57 1296 DNA Corynebacterium glutamicum CDS (101)..(1273) RXS02157 57 gggtggaatt ggcacgatgg tgctgccgga tgtttttgat cgggagaatt atcctgaagg 60 caccgttttt agaaaagacg acaaggatgg ggaactgtaa atg agc acg ctg gaa 115 Met Ser Thr Leu Glu 1 5 act tgg cca cag gtc att att aat acg tac ggc acc cca cca gtt gag 163 Thr Trp Pro Gln Val Ile Ile Asn Thr Tyr Gly Thr Pro Pro Val Glu 10 15 20 ctg gtg tcc ggc aag ggc gca acc gtc act gat gac cag ggc aat gtc 211 Leu Val Ser Gly Lys Gly Ala Thr Val Thr Asp Asp Gln Gly Asn Val 25 30 35 tac atc gac ttg ctc gcg ggc atc gca gtc aac gcg ttg ggc cac gcc 259 Tyr Ile Asp Leu Leu Ala Gly Ile Ala Val Asn Ala Leu Gly His Ala 40 45 50 cac ccg gcg atc atc gag gcg gtc acc aac cag atc ggc caa ctt ggt 307 His Pro Ala Ile Ile Glu Ala Val Thr Asn Gln Ile Gly Gln Leu Gly 55 60 65 cac gtc tca aac ttg ttc gca tcc agg ccc gtc gtc gag gtc gcc gag 355 His Val Ser Asn Leu Phe Ala Ser Arg Pro Val Val Glu Val Ala Glu 70 75 80 85 gag ctc atc aag cgt ttt tcg ctt gac gac gcc acc ctc gcc gcg caa 403 Glu Leu Ile Lys Arg Phe Ser Leu Asp Asp Ala Thr Leu Ala Ala Gln 90 95 100 acc cgg gtt ttc ttc tgc aac tcg ggc gcc gaa gca aac gag gct gct 451 Thr Arg Val Phe Phe Cys Asn Ser Gly Ala Glu Ala Asn Glu Ala Ala 105 110 115 ttc aag att gca cgc ttg act ggt cgt tcc cgg att ctg gct gca gtt 499 Phe Lys Ile Ala Arg Leu Thr Gly Arg Ser Arg Ile Leu Ala Ala Val 120 125 130 cat ggt ttc cac ggc cgc acc atg ggt tcc ctc gcg ctg act ggc cag 547 His Gly Phe His Gly Arg Thr Met Gly Ser Leu Ala Leu Thr Gly Gln 135 140 145 cca gac aag cgt gaa gcg ttc ctg cca atg cca agc ggt gtg gag ttc 595 Pro Asp Lys Arg Glu Ala Phe Leu Pro Met Pro Ser Gly Val Glu Phe 150 155 160 165 tac cct tac ggc gac acc gat tac ttg cgc aaa atg gta gaa acc aac 643 Tyr Pro Tyr Gly Asp Thr Asp Tyr Leu Arg Lys Met Val Glu Thr Asn 170 175 180 cca acg gat gtg gct gct atc ttc ctc gag cca atc cag ggt gaa acg 691 Pro Thr Asp Val Ala Ala Ile Phe Leu Glu Pro Ile Gln Gly Glu Thr 185 190 195 ggc gtt gtt cca gca cct gaa gga ttc ctc aag gca gtg cgc gag ctg 739 Gly Val Val Pro Ala Pro Glu Gly Phe Leu Lys Ala Val Arg Glu Leu 200 205 210 tgc gat gag tac ggc atc ttg atg atc acc gat gaa gtc cag act ggc 787 Cys Asp Glu Tyr Gly Ile Leu Met Ile Thr Asp Glu Val Gln Thr Gly 215 220 225 gtt ggc cgt acc ggc gat ttc ttt gca cat cag cac gat ggc gtt gtt 835 Val Gly Arg Thr Gly Asp Phe Phe Ala His Gln His Asp Gly Val Val 230 235 240 245 ccc gat gtg gtg acc atg gcc aag gga ctt ggc ggc ggt ctt ccc atc 883 Pro Asp Val Val Thr Met Ala Lys Gly Leu Gly Gly Gly Leu Pro Ile 250 255 260 ggt gct tgt ttg gcc act ggc cgt gca gct gaa ttg atg acc cca ggc 931 Gly Ala Cys Leu Ala Thr Gly Arg Ala Ala Glu Leu Met Thr Pro Gly 265 270 275 aag cac ggc acc act ttc ggt ggc aac cca gtt gct tgt gca gct gcc 979 Lys His Gly Thr Thr Phe Gly Gly Asn Pro Val Ala Cys Ala Ala Ala 280 285 290 aag gca gtg ctg tct gtt gtc gat gac gct ttc tgc gca gaa gtt gcc 1027 Lys Ala Val Leu Ser Val Val Asp Asp Ala Phe Cys Ala Glu Val Ala 295 300 305 cgc aag ggc gag ctg ttc aag gaa ctt ctt gcc aag gtt gac ggc gtt 1075 Arg Lys Gly Glu Leu Phe Lys Glu Leu Leu Ala Lys Val Asp Gly Val 310 315 320 325 gta gac gtc cgt ggc agg ggc ttg atg ttg ggc gtg gtg ctg gag cgc 1123 Val Asp Val Arg Gly Arg Gly Leu Met Leu Gly Val Val Leu Glu Arg 330 335 340 gac gtc gca aag caa gct gtt ctt gat ggt ttt aag cac ggc gtt att 1171 Asp Val Ala Lys Gln Ala Val Leu Asp Gly Phe Lys His Gly Val Ile 345 350 355 ttg aat gca ccg gcg gac aac att atc cgt ttg acc ccg ccg ctg gtg 1219 Leu Asn Ala Pro Ala Asp Asn Ile Ile Arg Leu Thr Pro Pro Leu Val 360 365 370 atc acc gac gaa gaa atc gca gac gca gtc aag gct att gcc gag aca 1267 Ile Thr Asp Glu Glu Ile Ala Asp Ala Val Lys Ala Ile Ala Glu Thr 375 380 385 atc gca taaaggactc aaacttatga ctt 1296 Ile Ala 390 58 391 PRT Corynebacterium glutamicum 58 Met Ser Thr Leu Glu Thr Trp Pro Gln Val Ile Ile Asn Thr Tyr Gly 1 5 10 15 Thr Pro Pro Val Glu Leu Val Ser Gly Lys Gly Ala Thr Val Thr Asp 20 25 30 Asp Gln Gly Asn Val Tyr Ile Asp Leu Leu Ala Gly Ile Ala Val Asn 35 40 45 Ala Leu Gly His Ala His Pro Ala Ile Ile Glu Ala Val Thr Asn Gln 50 55 60 Ile Gly Gln Leu Gly His Val Ser Asn Leu Phe Ala Ser Arg Pro Val 65 70 75 80 Val Glu Val Ala Glu Glu Leu Ile Lys Arg Phe Ser Leu Asp Asp Ala 85 90 95 Thr Leu Ala Ala Gln Thr Arg Val Phe Phe Cys Asn Ser Gly Ala Glu 100 105 110 Ala Asn Glu Ala Ala Phe Lys Ile Ala Arg Leu Thr Gly Arg Ser Arg 115 120 125 Ile Leu Ala Ala Val His Gly Phe His Gly Arg Thr Met Gly Ser Leu 130 135 140 Ala Leu Thr Gly Gln Pro Asp Lys Arg Glu Ala Phe Leu Pro Met Pro 145 150 155 160 Ser Gly Val Glu Phe Tyr Pro Tyr Gly Asp Thr Asp Tyr Leu Arg Lys 165 170 175 Met Val Glu Thr Asn Pro Thr Asp Val Ala Ala Ile Phe Leu Glu Pro 180 185 190 Ile Gln Gly Glu Thr Gly Val Val Pro Ala Pro Glu Gly Phe Leu Lys 195 200 205 Ala Val Arg Glu Leu Cys Asp Glu Tyr Gly Ile Leu Met Ile Thr Asp 210 215 220 Glu Val Gln Thr Gly Val Gly Arg Thr Gly Asp Phe Phe Ala His Gln 225 230 235 240 His Asp Gly Val Val Pro Asp Val Val Thr Met Ala Lys Gly Leu Gly 245 250 255 Gly Gly Leu Pro Ile Gly Ala Cys Leu Ala Thr Gly Arg Ala Ala Glu 260 265 270 Leu Met Thr Pro Gly Lys His Gly Thr Thr Phe Gly Gly Asn Pro Val 275 280 285 Ala Cys Ala Ala Ala Lys Ala Val Leu Ser Val Val Asp Asp Ala Phe 290 295 300 Cys Ala Glu Val Ala Arg Lys Gly Glu Leu Phe Lys Glu Leu Leu Ala 305 310 315 320 Lys Val Asp Gly Val Val Asp Val Arg Gly Arg Gly Leu Met Leu Gly 325 330 335 Val Val Leu Glu Arg Asp Val Ala Lys Gln Ala Val Leu Asp Gly Phe 340 345 350 Lys His Gly Val Ile Leu Asn Ala Pro Ala Asp Asn Ile Ile Arg Leu 355 360 365 Thr Pro Pro Leu Val Ile Thr Asp Glu Glu Ile Ala Asp Ala Val Lys 370 375 380 Ala Ile Ala Glu Thr Ile Ala 385 390 59 1008 DNA Corynebacterium glutamicum CDS (101)..(985) RXC00733 59 acggcgaggt tgtcggtatt ggaacgcaca cgaatttgct gaacacgtgc ggtacctacc 60 gtgaaattgt tgaatcccaa gagactgcgc aggcgcaatc atg agt aat act gca 115 Met Ser Asn Thr Ala 1 5 ggc ccc cgc ggg cgt tcc cat cag gca gac gcc gcg ccg aat caa aag 163 Gly Pro Arg Gly Arg Ser His Gln Ala Asp Ala Ala Pro Asn Gln Lys 10 15 20 gca cag aat ttc gga cca tct gcc aaa agg ctt ttc gga att cta ggc 211 Ala Gln Asn Phe Gly Pro Ser Ala Lys Arg Leu Phe Gly Ile Leu Gly 25 30 35 cat gac cgt aac acc tta att ttt gtt atc ttc cta gcc gtc ctg agc 259 His Asp Arg Asn Thr Leu Ile Phe Val Ile Phe Leu Ala Val Leu Ser 40 45 50 gtt gga ctt acc gtc ttg ggc cca tgg ttg ctg ggt aaa gcc acc aac 307 Val Gly Leu Thr Val Leu Gly Pro Trp Leu Leu Gly Lys Ala Thr Asn 55 60 65 gtg gtg ttt gaa gga ttc cta tct aag cgc atg ccg gct ggt gcg tca 355 Val Val Phe Glu Gly Phe Leu Ser Lys Arg Met Pro Ala Gly Ala Ser 70 75 80 85 aag gaa gat atc atc gcg cag ttg cag gct gca ggt aaa cat aat cag 403 Lys Glu Asp Ile Ile Ala Gln Leu Gln Ala Ala Gly Lys His Asn Gln 90 95 100 gct tcc atg atg gaa gac atg aac ctt gtt cca ggc tca ggc att gat 451 Ala Ser Met Met Glu Asp Met Asn Leu Val Pro Gly Ser Gly Ile Asp 105 110 115 ttt gaa aaa tta gcc atg atc ctc gga ctg gtg atc ggt gct tat ctc 499 Phe Glu Lys Leu Ala Met Ile Leu Gly Leu Val Ile Gly Ala Tyr Leu 120 125 130 atc ggt agc ctg ttg tcg ttg ttc cag gcg cgg atg ctc aac cgc atc 547 Ile Gly Ser Leu Leu Ser Leu Phe Gln Ala Arg Met Leu Asn Arg Ile 135 140 145 gtg caa agt gcc atg cac cgg ctg cgc atg gag gtg gag gaa aaa atc 595 Val Gln Ser Ala Met His Arg Leu Arg Met Glu Val Glu Glu Lys Ile 150 155 160 165 cac cgc cta ccg ctg agc tat ttc gat tcc atc aaa cgt ggt gat ctg 643 His Arg Leu Pro Leu Ser Tyr Phe Asp Ser Ile Lys Arg Gly Asp Leu 170 175 180 ctt agc cgt gtg acc aac gat gtg gat aat atc ggt caa tcc ctg caa 691 Leu Ser Arg Val Thr Asn Asp Val Asp Asn Ile Gly Gln Ser Leu Gln 185 190 195 caa acc ttg tca cag gcg atc act tcc cta ctg acc gtc atc ggt gtg 739 Gln Thr Leu Ser Gln Ala Ile Thr Ser Leu Leu Thr Val Ile Gly Val 200 205 210 ttg gtg atg atg ttt atc atc tcc cca ctg ctc gca ctc gtg gcg ctg 787 Leu Val Met Met Phe Ile Ile Ser Pro Leu Leu Ala Leu Val Ala Leu 215 220 225 gta tcc att ccg gtc acc atc gtg gtc act gtg gtg gtt gcg agc cgt 835 Val Ser Ile Pro Val Thr Ile Val Val Thr Val Val Val Ala Ser Arg 230 235 240 245 tcc cag aaa ctc ttt gcg gaa cag tgg aag cag acc ggt att ttg aat 883 Ser Gln Lys Leu Phe Ala Glu Gln Trp Lys Gln Thr Gly Ile Leu Asn 250 255 260 gcg cgc ctg gag gaa acc tac tct ggc cac gcc gtg gtt aag gtt ttc 931 Ala Arg Leu Glu Glu Thr Tyr Ser Gly His Ala Val Val Lys Val Phe 265 270 275 gga cac caa aag gat gtt caa gaa gca ttc gag gaa gaa aat caa gct 979 Gly His Gln Lys Asp Val Gln Glu Ala Phe Glu Glu Glu Asn Gln Ala 280 285 290 tgt gta taaggccagc tttggtgccc agt 1008 Cys Val 295 60 295 PRT Corynebacterium glutamicum 60 Met Ser Asn Thr Ala Gly Pro Arg Gly Arg Ser His Gln Ala Asp Ala 1 5 10 15 Ala Pro Asn Gln Lys Ala Gln Asn Phe Gly Pro Ser Ala Lys Arg Leu 20 25 30 Phe Gly Ile Leu Gly His Asp Arg Asn Thr Leu Ile Phe Val Ile Phe 35 40 45 Leu Ala Val Leu Ser Val Gly Leu Thr Val Leu Gly Pro Trp Leu Leu 50 55 60 Gly Lys Ala Thr Asn Val Val Phe Glu Gly Phe Leu Ser Lys Arg Met 65 70 75 80 Pro Ala Gly Ala Ser Lys Glu Asp Ile Ile Ala Gln Leu Gln Ala Ala 85 90 95 Gly Lys His Asn Gln Ala Ser Met Met Glu Asp Met Asn Leu Val Pro 100 105 110 Gly Ser Gly Ile Asp Phe Glu Lys Leu Ala Met Ile Leu Gly Leu Val 115 120 125 Ile Gly Ala Tyr Leu Ile Gly Ser Leu Leu Ser Leu Phe Gln Ala Arg 130 135 140 Met Leu Asn Arg Ile Val Gln Ser Ala Met His Arg Leu Arg Met Glu 145 150 155 160 Val Glu Glu Lys Ile His Arg Leu Pro Leu Ser Tyr Phe Asp Ser Ile 165 170 175 Lys Arg Gly Asp Leu Leu Ser Arg Val Thr Asn Asp Val Asp Asn Ile 180 185 190 Gly Gln Ser Leu Gln Gln Thr Leu Ser Gln Ala Ile Thr Ser Leu Leu 195 200 205 Thr Val Ile Gly Val Leu Val Met Met Phe Ile Ile Ser Pro Leu Leu 210 215 220 Ala Leu Val Ala Leu Val Ser Ile Pro Val Thr Ile Val Val Thr Val 225 230 235 240 Val Val Ala Ser Arg Ser Gln Lys Leu Phe Ala Glu Gln Trp Lys Gln 245 250 255 Thr Gly Ile Leu Asn Ala Arg Leu Glu Glu Thr Tyr Ser Gly His Ala 260 265 270 Val Val Lys Val Phe Gly His Gln Lys Asp Val Gln Glu Ala Phe Glu 275 280 285 Glu Glu Asn Gln Ala Cys Val 290 295 61 426 DNA Corynebacterium glutamicum CDS (1)..(426) RXC00861 61 atg gct cct cac aag gtc atg ctg att acc act ggt act cag ggt gag 48 Met Ala Pro His Lys Val Met Leu Ile Thr Thr Gly Thr Gln Gly Glu 1 5 10 15 cct atg gct gcg ctg tct cgc atg gcg cgt cgt gag cac cga cag atc 96 Pro Met Ala Ala Leu Ser Arg Met Ala Arg Arg Glu His Arg Gln Ile 20 25 30 act gtc cgt gat gga gac ttg att atc ctt tct tcc tcc ctg gtt cca 144 Thr Val Arg Asp Gly Asp Leu Ile Ile Leu Ser Ser Ser Leu Val Pro 35 40 45 ggt aac gaa gaa gca gtg ttc ggt gtc atc aac atg ctg gct cag atc 192 Gly Asn Glu Glu Ala Val Phe Gly Val Ile Asn Met Leu Ala Gln Ile 50 55 60 ggt gca act gtt gtt acc ggt cgc gac gcc aag gtg cac acc tcg ggc 240 Gly Ala Thr Val Val Thr Gly Arg Asp Ala Lys Val His Thr Ser Gly 65 70 75 80 cac ggc tac tcc gga gag ctg ttg ttc ttg tac aac gcc gct cgt ccg 288 His Gly Tyr Ser Gly Glu Leu Leu Phe Leu Tyr Asn Ala Ala Arg Pro 85 90 95 aag aac gct atg cct gtc cac ggc gag tgg cgc cac ctg cgc gcc aac 336 Lys Asn Ala Met Pro Val His Gly Glu Trp Arg His Leu Arg Ala Asn 100 105 110 aag gaa ctg gct atc tcc act ggt gtt aac cgc gac aac gtt gtg ctt 384 Lys Glu Leu Ala Ile Ser Thr Gly Val Asn Arg Asp Asn Val Val Leu 115 120 125 gca caa aac ggt gtt gtg gtt gat atg gtc aac ggt cgc gca 426 Ala Gln Asn Gly Val Val Val Asp Met Val Asn Gly Arg Ala 130 135 140 62 142 PRT Corynebacterium glutamicum 62 Met Ala Pro His Lys Val Met Leu Ile Thr Thr Gly Thr Gln Gly Glu 1 5 10 15 Pro Met Ala Ala Leu Ser Arg Met Ala Arg Arg Glu His Arg Gln Ile 20 25 30 Thr Val Arg Asp Gly Asp Leu Ile Ile Leu Ser Ser Ser Leu Val Pro 35 40 45 Gly Asn Glu Glu Ala Val Phe Gly Val Ile Asn Met Leu Ala Gln Ile 50 55 60 Gly Ala Thr Val Val Thr Gly Arg Asp Ala Lys Val His Thr Ser Gly 65 70 75 80 His Gly Tyr Ser Gly Glu Leu Leu Phe Leu Tyr Asn Ala Ala Arg Pro 85 90 95 Lys Asn Ala Met Pro Val His Gly Glu Trp Arg His Leu Arg Ala Asn 100 105 110 Lys Glu Leu Ala Ile Ser Thr Gly Val Asn Arg Asp Asn Val Val Leu 115 120 125 Ala Gln Asn Gly Val Val Val Asp Met Val Asn Gly Arg Ala 130 135 140 63 1066 DNA Corynebacterium glutamicum CDS (101)..(1066) RXC00866 63 gcatcaacgt aggagatcct cgacttccaa ttatggctcc aaatgagcag gaacttgagg 60 ctctccgaga agacatgaaa aaagctggag ttctataaat atg aat gat tcc cga 115 Met Asn Asp Ser Arg 1 5 aat cgc ggc cgg aag gtt acc cgc aag gcg ggc cca cca gaa gct ggt 163 Asn Arg Gly Arg Lys Val Thr Arg Lys Ala Gly Pro Pro Glu Ala Gly 10 15 20 cag gaa aac cat ctg gat acc cct gtc ttt cag gca cca gat gct tcc 211 Gln Glu Asn His Leu Asp Thr Pro Val Phe Gln Ala Pro Asp Ala Ser 25 30 35 tct aac cag agc gct gta aaa gct gag acc gcc gga aac gac aat cgg 259 Ser Asn Gln Ser Ala Val Lys Ala Glu Thr Ala Gly Asn Asp Asn Arg 40 45 50 gat gct gcg caa ggt gct caa gga tcc caa gat tct cag ggt tcc cag 307 Asp Ala Ala Gln Gly Ala Gln Gly Ser Gln Asp Ser Gln Gly Ser Gln 55 60 65 aac gct caa ggt tcc cag aac cgc gag tcc gga aac aac aac cgc aac 355 Asn Ala Gln Gly Ser Gln Asn Arg Glu Ser Gly Asn Asn Asn Arg Asn 70 75 80 85 cgt tcc aac aac aac cgt cgc ggt ggt cgt gga cgt cgt gga tcc gga 403 Arg Ser Asn Asn Asn Arg Arg Gly Gly Arg Gly Arg Arg Gly Ser Gly 90 95 100 aac gcc aat gag ggc gcg aac aac aac agc ggt aac cag aac cgt cag 451 Asn Ala Asn Glu Gly Ala Asn Asn Asn Ser Gly Asn Gln Asn Arg Gln 105 110 115 ggc gga aac cgt ggc aac cgc ggt ggc gga cgc cga aac gtt gtt aag 499 Gly Gly Asn Arg Gly Asn Arg Gly Gly Gly Arg Arg Asn Val Val Lys 120 125 130 tcg atg cag ggt gcg gat ctg acc cag cgc ctg cca gag cca cca aag 547 Ser Met Gln Gly Ala Asp Leu Thr Gln Arg Leu Pro Glu Pro Pro Lys 135 140 145 gca ccg gca aac ggt ctg cgt att tac gca ctt ggt ggc att tcc gaa 595 Ala Pro Ala Asn Gly Leu Arg Ile Tyr Ala Leu Gly Gly Ile Ser Glu 150 155 160 165 atc ggt cgc aac atg acc gtg ttt gag tac aac aac cgt ctg ctc atc 643 Ile Gly Arg Asn Met Thr Val Phe Glu Tyr Asn Asn Arg Leu Leu Ile 170 175 180 gtg gac tgt ggt gtg ctc ttc cca tct tca ggt gag cca ggc gtt gac 691 Val Asp Cys Gly Val Leu Phe Pro Ser Ser Gly Glu Pro Gly Val Asp 185 190 195 ctg att ctt cct gac ttc ggc cca att gag gat cac ctg cac cgc gtc 739 Leu Ile Leu Pro Asp Phe Gly Pro Ile Glu Asp His Leu His Arg Val 200 205 210 gat gca ttg gtg gtt act cac gga cac gaa gac cac att ggt gct att 787 Asp Ala Leu Val Val Thr His Gly His Glu Asp His Ile Gly Ala Ile 215 220 225 ccc tgg ctg ctg aag ctg cgc aac gat atc cca atc ttg gca tcc cgt 835 Pro Trp Leu Leu Lys Leu Arg Asn Asp Ile Pro Ile Leu Ala Ser Arg 230 235 240 245 ttc acc ttg gct ctg att gca gct aag tgt aag gaa cac cgt cag cgt 883 Phe Thr Leu Ala Leu Ile Ala Ala Lys Cys Lys Glu His Arg Gln Arg 250 255 260 ccg aag ctg atc gag gtc aac gag cag tcc aat gag gac cgc gga ccg 931 Pro Lys Leu Ile Glu Val Asn Glu Gln Ser Asn Glu Asp Arg Gly Pro 265 270 275 ttc aac att cgc ttc tgg gct gtt aac cac tcc atc cca gac tgc ctt 979 Phe Asn Ile Arg Phe Trp Ala Val Asn His Ser Ile Pro Asp Cys Leu 280 285 290 ggt ctt gct atc aag act cct gct ggt ttg gtc atc cac acc ggt gac 1027 Gly Leu Ala Ile Lys Thr Pro Ala Gly Leu Val Ile His Thr Gly Asp 295 300 305 atc aag ctg gat cag act cct cct gat gga cgc cca act 1066 Ile Lys Leu Asp Gln Thr Pro Pro Asp Gly Arg Pro Thr 310 315 320 64 322 PRT Corynebacterium glutamicum 64 Met Asn Asp Ser Arg Asn Arg Gly Arg Lys Val Thr Arg Lys Ala Gly 1 5 10 15 Pro Pro Glu Ala Gly Gln Glu Asn His Leu Asp Thr Pro Val Phe Gln 20 25 30 Ala Pro Asp Ala Ser Ser Asn Gln Ser Ala Val Lys Ala Glu Thr Ala 35 40 45 Gly Asn Asp Asn Arg Asp Ala Ala Gln Gly Ala Gln Gly Ser Gln Asp 50 55 60 Ser Gln Gly Ser Gln Asn Ala Gln Gly Ser Gln Asn Arg Glu Ser Gly 65 70 75 80 Asn Asn Asn Arg Asn Arg Ser Asn Asn Asn Arg Arg Gly Gly Arg Gly 85 90 95 Arg Arg Gly Ser Gly Asn Ala Asn Glu Gly Ala Asn Asn Asn Ser Gly 100 105 110 Asn Gln Asn Arg Gln Gly Gly Asn Arg Gly Asn Arg Gly Gly Gly Arg 115 120 125 Arg Asn Val Val Lys Ser Met Gln Gly Ala Asp Leu Thr Gln Arg Leu 130 135 140 Pro Glu Pro Pro Lys Ala Pro Ala Asn Gly Leu Arg Ile Tyr Ala Leu 145 150 155 160 Gly Gly Ile Ser Glu Ile Gly Arg Asn Met Thr Val Phe Glu Tyr Asn 165 170 175 Asn Arg Leu Leu Ile Val Asp Cys Gly Val Leu Phe Pro Ser Ser Gly 180 185 190 Glu Pro Gly Val Asp Leu Ile Leu Pro Asp Phe Gly Pro Ile Glu Asp 195 200 205 His Leu His Arg Val Asp Ala Leu Val Val Thr His Gly His Glu Asp 210 215 220 His Ile Gly Ala Ile Pro Trp Leu Leu Lys Leu Arg Asn Asp Ile Pro 225 230 235 240 Ile Leu Ala Ser Arg Phe Thr Leu Ala Leu Ile Ala Ala Lys Cys Lys 245 250 255 Glu His Arg Gln Arg Pro Lys Leu Ile Glu Val Asn Glu Gln Ser Asn 260 265 270 Glu Asp Arg Gly Pro Phe Asn Ile Arg Phe Trp Ala Val Asn His Ser 275 280 285 Ile Pro Asp Cys Leu Gly Leu Ala Ile Lys Thr Pro Ala Gly Leu Val 290 295 300 Ile His Thr Gly Asp Ile Lys Leu Asp Gln Thr Pro Pro Asp Gly Arg 305 310 315 320 Pro Thr 65 1527 DNA Corynebacterium glutamicum CDS (101)..(1504) RXC02095 65 ctctcttggt cctctcccca cccattttta agtactcaag acccttccaa cagaaaggat 60 tactccccca acaggctcaa aaatactgaa aggctcacgc atg aaa act gag caa 115 Met Lys Thr Glu Gln 1 5 tcc caa aaa gca caa tta gcc cct aag aaa gca cct gaa aag cca caa 163 Ser Gln Lys Ala Gln Leu Ala Pro Lys Lys Ala Pro Glu Lys Pro Gln 10 15 20 cgc atc cgc caa ctt att tcc gtg gcg tgg cag cga cct tgg ctc acc 211 Arg Ile Arg Gln Leu Ile Ser Val Ala Trp Gln Arg Pro Trp Leu Thr 25 30 35 tca ttc acc gta atc agc gct tta gct gca acg ttg ttt gaa ctt aca 259 Ser Phe Thr Val Ile Ser Ala Leu Ala Ala Thr Leu Phe Glu Leu Thr 40 45 50 ctt cct ctt ttg acc ggt ggc gcc atc gat atc gcg ctc gga aat acc 307 Leu Pro Leu Leu Thr Gly Gly Ala Ile Asp Ile Ala Leu Gly Asn Thr 55 60 65 gga gat act tta acc act gac ctg ctg gac cgg ttc act ccg agt gga 355 Gly Asp Thr Leu Thr Thr Asp Leu Leu Asp Arg Phe Thr Pro Ser Gly 70 75 80 85 tta agc gtg ttg acc agc gtc att gcc ctt atc gtg ctt ctc gcg ttg 403 Leu Ser Val Leu Thr Ser Val Ile Ala Leu Ile Val Leu Leu Ala Leu 90 95 100 ctt cgc tat gcc agt caa ttt gga cgg cga tac acc gca ggc aag ctc 451 Leu Arg Tyr Ala Ser Gln Phe Gly Arg Arg Tyr Thr Ala Gly Lys Leu 105 110 115 agc atg ggg gta cag cat gat gtc cgg ctt aaa acg atg cgc tca ttg 499 Ser Met Gly Val Gln His Asp Val Arg Leu Lys Thr Met Arg Ser Leu 120 125 130 cag aac ctc gat ggg cca ggt cag gac tct att cgc aca ggc caa gta 547 Gln Asn Leu Asp Gly Pro Gly Gln Asp Ser Ile Arg Thr Gly Gln Val 135 140 145 gtc agt cgg tcc att tcg gat atc aac atg gtg caa agc ctt gtg gcg 595 Val Ser Arg Ser Ile Ser Asp Ile Asn Met Val Gln Ser Leu Val Ala 150 155 160 165 atg ttg ccg atg ttg atc gga aat gtg gtc aag ctt gtg ctc act ttg 643 Met Leu Pro Met Leu Ile Gly Asn Val Val Lys Leu Val Leu Thr Leu 170 175 180 gtg atc atg ctg gct att tcc ccg ccg ctg acc atc atc gct gca gtg 691 Val Ile Met Leu Ala Ile Ser Pro Pro Leu Thr Ile Ile Ala Ala Val 185 190 195 ttg gtg cct ttg ctg ttg tgg gcc gtg gcc tat tcg cga aaa gcg ctt 739 Leu Val Pro Leu Leu Leu Trp Ala Val Ala Tyr Ser Arg Lys Ala Leu 200 205 210 ttt gcg tcc acg tgg tcg gcc cag caa aag gct gcg gat ctg acc act 787 Phe Ala Ser Thr Trp Ser Ala Gln Gln Lys Ala Ala Asp Leu Thr Thr 215 220 225 cat gtg gaa gaa act gtc acg ggt atc cgc gtg gtc aag gca ttt gcg 835 His Val Glu Glu Thr Val Thr Gly Ile Arg Val Val Lys Ala Phe Ala 230 235 240 245 cag gaa gac cgc gag acc gac aaa ttg gat ctc acc gca cgt gag tta 883 Gln Glu Asp Arg Glu Thr Asp Lys Leu Asp Leu Thr Ala Arg Glu Leu 250 255 260 ttt gcc cag cgc atg cgc act gca cgt ctg acg gca aag ttc atc ccc 931 Phe Ala Gln Arg Met Arg Thr Ala Arg Leu Thr Ala Lys Phe Ile Pro 265 270 275 atg gtt gag cag ctt ccg cag ctt gct ttg gtg gtc aac att gtt ggc 979 Met Val Glu Gln Leu Pro Gln Leu Ala Leu Val Val Asn Ile Val Gly 280 285 290 ggt ggc tat ttg gcc atg act ggt cac atc acg gtg ggc acg ttt gtg 1027 Gly Gly Tyr Leu Ala Met Thr Gly His Ile Thr Val Gly Thr Phe Val 295 300 305 gcg ttt tct tcc tat ctc act agc ttg tcg gcg gtg gct agg tcc ctg 1075 Ala Phe Ser Ser Tyr Leu Thr Ser Leu Ser Ala Val Ala Arg Ser Leu 310 315 320 325 tcg ggc atg ctc atg cgc gtg cag ttg gcg ctg tct tct gtg gag cgc 1123 Ser Gly Met Leu Met Arg Val Gln Leu Ala Leu Ser Ser Val Glu Arg 330 335 340 atc ttt gaa gtc att gat ctt cag cct gaa cgc acc gat cct gca cac 1171 Ile Phe Glu Val Ile Asp Leu Gln Pro Glu Arg Thr Asp Pro Ala His 345 350 355 ccc ctg tca ctt ccc gac act ccc ctg ggt ctg tcg ttc aac aac gta 1219 Pro Leu Ser Leu Pro Asp Thr Pro Leu Gly Leu Ser Phe Asn Asn Val 360 365 370 gat ttc cgt ggg att ctc aac ggt ttt gag ctg ggt gtt cag gcc ggt 1267 Asp Phe Arg Gly Ile Leu Asn Gly Phe Glu Leu Gly Val Gln Ala Gly 375 380 385 gaa acc gtt gtg ttg gtg ggc cct cca ggt tca ggc aag acc atg gct 1315 Glu Thr Val Val Leu Val Gly Pro Pro Gly Ser Gly Lys Thr Met Ala 390 395 400 405 gtg cag ctt gct gga aac ttt tat caa cca gac agc ggc cac atc gcc 1363 Val Gln Leu Ala Gly Asn Phe Tyr Gln Pro Asp Ser Gly His Ile Ala 410 415 420 ttt gat agc aac ggc cat cgc act cgc ttc gac gac ctc acc cac agc 1411 Phe Asp Ser Asn Gly His Arg Thr Arg Phe Asp Asp Leu Thr His Ser 425 430 435 gat atc cgc agg aat ctc atc gcg gtt ttt gat gag ccg ttc ttg tac 1459 Asp Ile Arg Arg Asn Leu Ile Ala Val Phe Asp Glu Pro Phe Leu Tyr 440 445 450 tcc tcc tcc ata ccg cga gaa cat ctc gat ggg ttt gga tgt cag 1504 Ser Ser Ser Ile Pro Arg Glu His Leu Asp Gly Phe Gly Cys Gln 455 460 465 tgatgagcag atcgaacacg cag 1527 66 468 PRT Corynebacterium glutamicum 66 Met Lys Thr Glu Gln Ser Gln Lys Ala Gln Leu Ala Pro Lys Lys Ala 1 5 10 15 Pro Glu Lys Pro Gln Arg Ile Arg Gln Leu Ile Ser Val Ala Trp Gln 20 25 30 Arg Pro Trp Leu Thr Ser Phe Thr Val Ile Ser Ala Leu Ala Ala Thr 35 40 45 Leu Phe Glu Leu Thr Leu Pro Leu Leu Thr Gly Gly Ala Ile Asp Ile 50 55 60 Ala Leu Gly Asn Thr Gly Asp Thr Leu Thr Thr Asp Leu Leu Asp Arg 65 70 75 80 Phe Thr Pro Ser Gly Leu Ser Val Leu Thr Ser Val Ile Ala Leu Ile 85 90 95 Val Leu Leu Ala Leu Leu Arg Tyr Ala Ser Gln Phe Gly Arg Arg Tyr 100 105 110 Thr Ala Gly Lys Leu Ser Met Gly Val Gln His Asp Val Arg Leu Lys 115 120 125 Thr Met Arg Ser Leu Gln Asn Leu Asp Gly Pro Gly Gln Asp Ser Ile 130 135 140 Arg Thr Gly Gln Val Val Ser Arg Ser Ile Ser Asp Ile Asn Met Val 145 150 155 160 Gln Ser Leu Val Ala Met Leu Pro Met Leu Ile Gly Asn Val Val Lys 165 170 175 Leu Val Leu Thr Leu Val Ile Met Leu Ala Ile Ser Pro Pro Leu Thr 180 185 190 Ile Ile Ala Ala Val Leu Val Pro Leu Leu Leu Trp Ala Val Ala Tyr 195 200 205 Ser Arg Lys Ala Leu Phe Ala Ser Thr Trp Ser Ala Gln Gln Lys Ala 210 215 220 Ala Asp Leu Thr Thr His Val Glu Glu Thr Val Thr Gly Ile Arg Val 225 230 235 240 Val Lys Ala Phe Ala Gln Glu Asp Arg Glu Thr Asp Lys Leu Asp Leu 245 250 255 Thr Ala Arg Glu Leu Phe Ala Gln Arg Met Arg Thr Ala Arg Leu Thr 260 265 270 Ala Lys Phe Ile Pro Met Val Glu Gln Leu Pro Gln Leu Ala Leu Val 275 280 285 Val Asn Ile Val Gly Gly Gly Tyr Leu Ala Met Thr Gly His Ile Thr 290 295 300 Val Gly Thr Phe Val Ala Phe Ser Ser Tyr Leu Thr Ser Leu Ser Ala 305 310 315 320 Val Ala Arg Ser Leu Ser Gly Met Leu Met Arg Val Gln Leu Ala Leu 325 330 335 Ser Ser Val Glu Arg Ile Phe Glu Val Ile Asp Leu Gln Pro Glu Arg 340 345 350 Thr Asp Pro Ala His Pro Leu Ser Leu Pro Asp Thr Pro Leu Gly Leu 355 360 365 Ser Phe Asn Asn Val Asp Phe Arg Gly Ile Leu Asn Gly Phe Glu Leu 370 375 380 Gly Val Gln Ala Gly Glu Thr Val Val Leu Val Gly Pro Pro Gly Ser 385 390 395 400 Gly Lys Thr Met Ala Val Gln Leu Ala Gly Asn Phe Tyr Gln Pro Asp 405 410 415 Ser Gly His Ile Ala Phe Asp Ser Asn Gly His Arg Thr Arg Phe Asp 420 425 430 Asp Leu Thr His Ser Asp Ile Arg Arg Asn Leu Ile Ala Val Phe Asp 435 440 445 Glu Pro Phe Leu Tyr Ser Ser Ser Ile Pro Arg Glu His Leu Asp Gly 450 455 460 Phe Gly Cys Gln 465 67 295 DNA Corynebacterium glutamicum CDS (84)..(272) RXC03185 67 agcgcccaac cgttcagacc agcggtttct ctgaggatgc aaagtccatg atgggtnagg 60 tcactgagct gtccgaaacc acc atg aat gat ctt gca gct gaa ggt gaa aac 113 Met Asn Asp Leu Ala Ala Glu Gly Glu Asn 1 5 10 gat cct tac cgc atg gtt cag cag ctg cgc cgc aag ctc tct cgc ttc 161 Asp Pro Tyr Arg Met Val Gln Gln Leu Arg Arg Lys Leu Ser Arg Phe 15 20 25 gtc gag cag aag tgg aag cgc cag ccg gtc atc atg cca acc gtc att 209 Val Glu Gln Lys Trp Lys Arg Gln Pro Val Ile Met Pro Thr Val Ile 30 35 40 ccg atg act gcg gaa acc acg cac atc ggt gac gat gag gtt cgc gct 257 Pro Met Thr Ala Glu Thr Thr His Ile Gly Asp Asp Glu Val Arg Ala 45 50 55 tca cgc gag tcc ctg taaaagcatt tcgcttttcg acg 295 Ser Arg Glu Ser Leu 60 68 63 PRT Corynebacterium glutamicum 68 Met Asn Asp Leu Ala Ala Glu Gly Glu Asn Asp Pro Tyr Arg Met Val 1 5 10 15 Gln Gln Leu Arg Arg Lys Leu Ser Arg Phe Val Glu Gln Lys Trp Lys 20 25 30 Arg Gln Pro Val Ile Met Pro Thr Val Ile Pro Met Thr Ala Glu Thr 35 40 45 Thr His Ile Gly Asp Asp Glu Val Arg Ala Ser Arg Glu Ser Leu 50 55 60 69 1170 DNA Corynebacterium glutamicum CDS (101)..(1147) RXA00115 69 tggattctcg agtctgtaca cccttgatca aagcccgagt gttccgtaga ttaactttgt 60 cgtatattgt gacctacacc ccatactgtt aggagttttc atg ctc gac aat agt 115 Met Leu Asp Asn Ser 1 5 ttt tac acc gca gag gtt cag ggc cca tac gaa acc gct tcc att ggc 163 Phe Tyr Thr Ala Glu Val Gln Gly Pro Tyr Glu Thr Ala Ser Ile Gly 10 15 20 cgg ctc gaa ctc gaa gaa ggg ggt gtg att gag gat tgc tgg ttg gct 211 Arg Leu Glu Leu Glu Glu Gly Gly Val Ile Glu Asp Cys Trp Leu Ala 25 30 35 tac gct aca gct gga acg ctc aac gag gac aag tcc aac gcc atc ctc 259 Tyr Ala Thr Ala Gly Thr Leu Asn Glu Asp Lys Ser Asn Ala Ile Leu 40 45 50 att ccg acg tgg tac tcc gga acc cat cag acc tgg ttc cag cag tac 307 Ile Pro Thr Trp Tyr Ser Gly Thr His Gln Thr Trp Phe Gln Gln Tyr 55 60 65 atc ggc act gat cat gcg ctg gat cca tca aag tat ttc atc atc tcc 355 Ile Gly Thr Asp His Ala Leu Asp Pro Ser Lys Tyr Phe Ile Ile Ser 70 75 80 85 atc aac caa atc ggt aat ggt ttg tcg gtc tcc cct gcc aac acg gct 403 Ile Asn Gln Ile Gly Asn Gly Leu Ser Val Ser Pro Ala Asn Thr Ala 90 95 100 gat gac agc atc tcg atg tcc aag ttc ccg aat gtt cgc att ggt gat 451 Asp Asp Ser Ile Ser Met Ser Lys Phe Pro Asn Val Arg Ile Gly Asp 105 110 115 gat gtc gtt gcc cag gac cgg ctc ttg cgc caa gag ttt ggt att acc 499 Asp Val Val Ala Gln Asp Arg Leu Leu Arg Gln Glu Phe Gly Ile Thr 120 125 130 gag ctc ttt gcc gtc gtt ggt ggt tcg atg ggt gcg cag caa acc tat 547 Glu Leu Phe Ala Val Val Gly Gly Ser Met Gly Ala Gln Gln Thr Tyr 135 140 145 gag tgg att gtt cgc ttc cct gac caa gtt cat cga gca gct ccg atc 595 Glu Trp Ile Val Arg Phe Pro Asp Gln Val His Arg Ala Ala Pro Ile 150 155 160 165 gcg ggc act gcg aag aac act cct cat gat ttc atc ttc acc cag act 643 Ala Gly Thr Ala Lys Asn Thr Pro His Asp Phe Ile Phe Thr Gln Thr 170 175 180 ctt aat gag acc gtt gag gcc gat cca ggg ttc aat ggc ggc gaa tac 691 Leu Asn Glu Thr Val Glu Ala Asp Pro Gly Phe Asn Gly Gly Glu Tyr 185 190 195 tcc tcc cat gaa gag gta gct gat gga ctt cgc cgt caa tcg cat ctt 739 Ser Ser His Glu Glu Val Ala Asp Gly Leu Arg Arg Gln Ser His Leu 200 205 210 tgg gct gcc atg gga ttt tcc aca gag ttc tgg aag cag gag gca tgg 787 Trp Ala Ala Met Gly Phe Ser Thr Glu Phe Trp Lys Gln Glu Ala Trp 215 220 225 cgt cgc ctg gga ctt gaa agt aag gag tca gtg ctc gcg gac ttc ctg 835 Arg Arg Leu Gly Leu Glu Ser Lys Glu Ser Val Leu Ala Asp Phe Leu 230 235 240 245 gat ccg ctg ttc atg tcc atg gat cct aat acc ttg ctc aac aac gct 883 Asp Pro Leu Phe Met Ser Met Asp Pro Asn Thr Leu Leu Asn Asn Ala 250 255 260 tgg aag tgg cag cat ggc gat gtc tct cgc cac acc ggc ggc gac ttg 931 Trp Lys Trp Gln His Gly Asp Val Ser Arg His Thr Gly Gly Asp Leu 265 270 275 gca gcg gct ctt ggc cga gtg aag gct aag acc ttc gtt atg ccc atc 979 Ala Ala Ala Leu Gly Arg Val Lys Ala Lys Thr Phe Val Met Pro Ile 280 285 290 agc gag gac atg ttc ttt cct gtt cgt gac tgt gcc gca gaa caa gca 1027 Ser Glu Asp Met Phe Phe Pro Val Arg Asp Cys Ala Ala Glu Gln Ala 295 300 305 ctc atc cca ggc agc gag ctt cga gtg atc gaa gac atc gcc ggt cac 1075 Leu Ile Pro Gly Ser Glu Leu Arg Val Ile Glu Asp Ile Ala Gly His 310 315 320 325 ctt ggg ctt ttt aac gtc tct gag aat tac atc cca cag atc gac aaa 1123 Leu Gly Leu Phe Asn Val Ser Glu Asn Tyr Ile Pro Gln Ile Asp Lys 330 335 340 aat ctg aaa gag ctg ttc gag agc taaacactga tgtcaaagag cct 1170 Asn Leu Lys Glu Leu Phe Glu Ser 345 70 349 PRT Corynebacterium glutamicum 70 Met Leu Asp Asn Ser Phe Tyr Thr Ala Glu Val Gln Gly Pro Tyr Glu 1 5 10 15 Thr Ala Ser Ile Gly Arg Leu Glu Leu Glu Glu Gly Gly Val Ile Glu 20 25 30 Asp Cys Trp Leu Ala Tyr Ala Thr Ala Gly Thr Leu Asn Glu Asp Lys 35 40 45 Ser Asn Ala Ile Leu Ile Pro Thr Trp Tyr Ser Gly Thr His Gln Thr 50 55 60 Trp Phe Gln Gln Tyr Ile Gly Thr Asp His Ala Leu Asp Pro Ser Lys 65 70 75 80 Tyr Phe Ile Ile Ser Ile Asn Gln Ile Gly Asn Gly Leu Ser Val Ser 85 90 95 Pro Ala Asn Thr Ala Asp Asp Ser Ile Ser Met Ser Lys Phe Pro Asn 100 105 110 Val Arg Ile Gly Asp Asp Val Val Ala Gln Asp Arg Leu Leu Arg Gln 115 120 125 Glu Phe Gly Ile Thr Glu Leu Phe Ala Val Val Gly Gly Ser Met Gly 130 135 140 Ala Gln Gln Thr Tyr Glu Trp Ile Val Arg Phe Pro Asp Gln Val His 145 150 155 160 Arg Ala Ala Pro Ile Ala Gly Thr Ala Lys Asn Thr Pro His Asp Phe 165 170 175 Ile Phe Thr Gln Thr Leu Asn Glu Thr Val Glu Ala Asp Pro Gly Phe 180 185 190 Asn Gly Gly Glu Tyr Ser Ser His Glu Glu Val Ala Asp Gly Leu Arg 195 200 205 Arg Gln Ser His Leu Trp Ala Ala Met Gly Phe Ser Thr Glu Phe Trp 210 215 220 Lys Gln Glu Ala Trp Arg Arg Leu Gly Leu Glu Ser Lys Glu Ser Val 225 230 235 240 Leu Ala Asp Phe Leu Asp Pro Leu Phe Met Ser Met Asp Pro Asn Thr 245 250 255 Leu Leu Asn Asn Ala Trp Lys Trp Gln His Gly Asp Val Ser Arg His 260 265 270 Thr Gly Gly Asp Leu Ala Ala Ala Leu Gly Arg Val Lys Ala Lys Thr 275 280 285 Phe Val Met Pro Ile Ser Glu Asp Met Phe Phe Pro Val Arg Asp Cys 290 295 300 Ala Ala Glu Gln Ala Leu Ile Pro Gly Ser Glu Leu Arg Val Ile Glu 305 310 315 320 Asp Ile Ala Gly His Leu Gly Leu Phe Asn Val Ser Glu Asn Tyr Ile 325 330 335 Pro Gln Ile Asp Lys Asn Leu Lys Glu Leu Phe Glu Ser 340 345 71 1254 DNA Corynebacterium glutamicum CDS (101)..(1231) RXN00403 71 tttttcagac tcgtgagaat gcaaactaga ctagacagag ctgtccatat acactggacg 60 aagttttagt cttgtccacc cagaacaggc ggttattttc atg ccc acc ctc gcg 115 Met Pro Thr Leu Ala 1 5 cct tca ggt caa ctt gaa atc caa gcg atc ggt gat gtc tcc acc gaa 163 Pro Ser Gly Gln Leu Glu Ile Gln Ala Ile Gly Asp Val Ser Thr Glu 10 15 20 gcc gga gca atc att aca aac gct gaa atc gcc tat cac cgc tgg ggt 211 Ala Gly Ala Ile Ile Thr Asn Ala Glu Ile Ala Tyr His Arg Trp Gly 25 30 35 gaa tac cgc gta gat aaa gaa gga cgc agc aat gtc gtt ctc atc gaa 259 Glu Tyr Arg Val Asp Lys Glu Gly Arg Ser Asn Val Val Leu Ile Glu 40 45 50 cac gcc ctc act gga gat tcc aac gca gcc gat tgg tgg gct gac ttg 307 His Ala Leu Thr Gly Asp Ser Asn Ala Ala Asp Trp Trp Ala Asp Leu 55 60 65 ctc ggt ccc ggc aaa gcc atc aac act gat att tac tgc gtg atc tgt 355 Leu Gly Pro Gly Lys Ala Ile Asn Thr Asp Ile Tyr Cys Val Ile Cys 70 75 80 85 acc aac gtc atc ggt ggt tgc aac ggt tcc acc gga cct ggc tcc atg 403 Thr Asn Val Ile Gly Gly Cys Asn Gly Ser Thr Gly Pro Gly Ser Met 90 95 100 cat cca gat gga aat ttc tgg ggt aat cgc ttc ccc gcc acg tcc att 451 His Pro Asp Gly Asn Phe Trp Gly Asn Arg Phe Pro Ala Thr Ser Ile 105 110 115 cgt gat cag gta aac gcc gaa aaa caa ttc ctc gac gca ctc ggc atc 499 Arg Asp Gln Val Asn Ala Glu Lys Gln Phe Leu Asp Ala Leu Gly Ile 120 125 130 acc acg gtc gcc gca gta ctt ggt ggt tcc atg ggt ggt gcc cgc acc 547 Thr Thr Val Ala Ala Val Leu Gly Gly Ser Met Gly Gly Ala Arg Thr 135 140 145 cta gag tgg gcc gca atg tac cca gaa act gtt ggc gca gct gct gtt 595 Leu Glu Trp Ala Ala Met Tyr Pro Glu Thr Val Gly Ala Ala Ala Val 150 155 160 165 ctt gca gtt tct gca cgc gcc agc gcc tgg caa atc ggc att caa tcc 643 Leu Ala Val Ser Ala Arg Ala Ser Ala Trp Gln Ile Gly Ile Gln Ser 170 175 180 gcc caa att aag gcg att gaa aac gac cac cac tgg cac gaa ggc aac 691 Ala Gln Ile Lys Ala Ile Glu Asn Asp His His Trp His Glu Gly Asn 185 190 195 tac tac gaa tcc ggc tgc aac cca gcc acc gga ctc ggc gcc gcc cga 739 Tyr Tyr Glu Ser Gly Cys Asn Pro Ala Thr Gly Leu Gly Ala Ala Arg 200 205 210 cgc atc gcc cac ctc acc tac cgt ggc gaa cta gaa atc gac gaa cgc 787 Arg Ile Ala His Leu Thr Tyr Arg Gly Glu Leu Glu Ile Asp Glu Arg 215 220 225 ttc ggc acc aaa gcc caa aag aac gaa aac cca ctc ggt ccc tac cgc 835 Phe Gly Thr Lys Ala Gln Lys Asn Glu Asn Pro Leu Gly Pro Tyr Arg 230 235 240 245 aag ccc gac cag cgc ttc gcc gtg gaa tcc tac ttg gac tac caa gca 883 Lys Pro Asp Gln Arg Phe Ala Val Glu Ser Tyr Leu Asp Tyr Gln Ala 250 255 260 gac aag cta gta cag cgt ttc gac gcc ggc tcc tac gtc ttg ctc acc 931 Asp Lys Leu Val Gln Arg Phe Asp Ala Gly Ser Tyr Val Leu Leu Thr 265 270 275 gac gcc ctc aac cgc cac gac att ggt cgc gac cgc gga ggc ctc aac 979 Asp Ala Leu Asn Arg His Asp Ile Gly Arg Asp Arg Gly Gly Leu Asn 280 285 290 aag gca ctc gaa tcc atc aaa gtt cca gtc ctt gtc gca ggc gta gat 1027 Lys Ala Leu Glu Ser Ile Lys Val Pro Val Leu Val Ala Gly Val Asp 295 300 305 acc gat att ttg tac ccc tac cac cag caa gaa cac ctc tcc aga aac 1075 Thr Asp Ile Leu Tyr Pro Tyr His Gln Gln Glu His Leu Ser Arg Asn 310 315 320 325 ctg gga aat cta ctg gca atg gca aaa atc gta tcc cct gtc ggc cac 1123 Leu Gly Asn Leu Leu Ala Met Ala Lys Ile Val Ser Pro Val Gly His 330 335 340 gat gct ttc ctc acc gaa agc cgc caa atg gat cgc atc gtg agg aac 1171 Asp Ala Phe Leu Thr Glu Ser Arg Gln Met Asp Arg Ile Val Arg Asn 345 350 355 ttc ttc agc ctc atc tcc cca gac gaa gac aac cct tcg acc tac atc 1219 Phe Phe Ser Leu Ile Ser Pro Asp Glu Asp Asn Pro Ser Thr Tyr Ile 360 365 370 gag ttc tac atc taataggtat ttacgacaaa tag 1254 Glu Phe Tyr Ile 375 72 377 PRT Corynebacterium glutamicum 72 Met Pro Thr Leu Ala Pro Ser Gly Gln Leu Glu Ile Gln Ala Ile Gly 1 5 10 15 Asp Val Ser Thr Glu Ala Gly Ala Ile Ile Thr Asn Ala Glu Ile Ala 20 25 30 Tyr His Arg Trp Gly Glu Tyr Arg Val Asp Lys Glu Gly Arg Ser Asn 35 40 45 Val Val Leu Ile Glu His Ala Leu Thr Gly Asp Ser Asn Ala Ala Asp 50 55 60 Trp Trp Ala Asp Leu Leu Gly Pro Gly Lys Ala Ile Asn Thr Asp Ile 65 70 75 80 Tyr Cys Val Ile Cys Thr Asn Val Ile Gly Gly Cys Asn Gly Ser Thr 85 90 95 Gly Pro Gly Ser Met His Pro Asp Gly Asn Phe Trp Gly Asn Arg Phe 100 105 110 Pro Ala Thr Ser Ile Arg Asp Gln Val Asn Ala Glu Lys Gln Phe Leu 115 120 125 Asp Ala Leu Gly Ile Thr Thr Val Ala Ala Val Leu Gly Gly Ser Met 130 135 140 Gly Gly Ala Arg Thr Leu Glu Trp Ala Ala Met Tyr Pro Glu Thr Val 145 150 155 160 Gly Ala Ala Ala Val Leu Ala Val Ser Ala Arg Ala Ser Ala Trp Gln 165 170 175 Ile Gly Ile Gln Ser Ala Gln Ile Lys Ala Ile Glu Asn Asp His His 180 185 190 Trp His Glu Gly Asn Tyr Tyr Glu Ser Gly Cys Asn Pro Ala Thr Gly 195 200 205 Leu Gly Ala Ala Arg Arg Ile Ala His Leu Thr Tyr Arg Gly Glu Leu 210 215 220 Glu Ile Asp Glu Arg Phe Gly Thr Lys Ala Gln Lys Asn Glu Asn Pro 225 230 235 240 Leu Gly Pro Tyr Arg Lys Pro Asp Gln Arg Phe Ala Val Glu Ser Tyr 245 250 255 Leu Asp Tyr Gln Ala Asp Lys Leu Val Gln Arg Phe Asp Ala Gly Ser 260 265 270 Tyr Val Leu Leu Thr Asp Ala Leu Asn Arg His Asp Ile Gly Arg Asp 275 280 285 Arg Gly Gly Leu Asn Lys Ala Leu Glu Ser Ile Lys Val Pro Val Leu 290 295 300 Val Ala Gly Val Asp Thr Asp Ile Leu Tyr Pro Tyr His Gln Gln Glu 305 310 315 320 His Leu Ser Arg Asn Leu Gly Asn Leu Leu Ala Met Ala Lys Ile Val 325 330 335 Ser Pro Val Gly His Asp Ala Phe Leu Thr Glu Ser Arg Gln Met Asp 340 345 350 Arg Ile Val Arg Asn Phe Phe Ser Leu Ile Ser Pro Asp Glu Asp Asn 355 360 365 Pro Ser Thr Tyr Ile Glu Phe Tyr Ile 370 375 73 1210 DNA Corynebacterium glutamicum CDS (101)..(1210) FRXA00403 73 tttttcagac tcgtgagaat gcaaactaga ctagacagag ctgtccatat acactggacg 60 aagttttagt cttgtccacc cagaacaggc ggttattttc atg ccc acc ctc gcg 115 Met Pro Thr Leu Ala 1 5 cct tca ggt caa ctt gaa atc caa gcg atc ggt gat gtc tcc acc gaa 163 Pro Ser Gly Gln Leu Glu Ile Gln Ala Ile Gly Asp Val Ser Thr Glu 10 15 20 gcc gga gca atc att aca aac gct gaa atc gcc tat cac cgc tgg ggt 211 Ala Gly Ala Ile Ile Thr Asn Ala Glu Ile Ala Tyr His Arg Trp Gly 25 30 35 gaa tac cgc gta gat aaa gaa gga cgc agc aat gtc gtt ctc atc gaa 259 Glu Tyr Arg Val Asp Lys Glu Gly Arg Ser Asn Val Val Leu Ile Glu 40 45 50 cac gcc ctc act gga gat tcc aac gca gcc gat tgg tgg gct gac ttg 307 His Ala Leu Thr Gly Asp Ser Asn Ala Ala Asp Trp Trp Ala Asp Leu 55 60 65 ctc ggt ccc ggc aaa gcc atc aac act gat att tac tgc gtg atc tgt 355 Leu Gly Pro Gly Lys Ala Ile Asn Thr Asp Ile Tyr Cys Val Ile Cys 70 75 80 85 acc aac gtc atc ggt ggt tgc aac ggt tcc acc gga cct ggc tcc atg 403 Thr Asn Val Ile Gly Gly Cys Asn Gly Ser Thr Gly Pro Gly Ser Met 90 95 100 cat cca gat gga aat ttc tgg ggt aat cgc ttc ccc gcc acg tcc att 451 His Pro Asp Gly Asn Phe Trp Gly Asn Arg Phe Pro Ala Thr Ser Ile 105 110 115 cgt gat cag gta aac gcc gaa aaa caa ttc ctc gac gca ctc ggc atc 499 Arg Asp Gln Val Asn Ala Glu Lys Gln Phe Leu Asp Ala Leu Gly Ile 120 125 130 acc acg gtc gcc gca gta ctt ggt ggt tcc atg ggt ggt gcc cgc acc 547 Thr Thr Val Ala Ala Val Leu Gly Gly Ser Met Gly Gly Ala Arg Thr 135 140 145 cta gag tgg gcc gca atg tac cca gaa act gtt ggc gca gct gct gtt 595 Leu Glu Trp Ala Ala Met Tyr Pro Glu Thr Val Gly Ala Ala Ala Val 150 155 160 165 ctt gca gtt tct gca cgc gcc agc gcc tgg caa atc ggc att caa tcc 643 Leu Ala Val Ser Ala Arg Ala Ser Ala Trp Gln Ile Gly Ile Gln Ser 170 175 180 gcc caa att aag gcg att gaa aac gac cac cac tgg cac gaa ggc aac 691 Ala Gln Ile Lys Ala Ile Glu Asn Asp His His Trp His Glu Gly Asn 185 190 195 tac tac gaa tcc ggc tgc aac cca gcc acc gga ctc ggc gcc gcc cga 739 Tyr Tyr Glu Ser Gly Cys Asn Pro Ala Thr Gly Leu Gly Ala Ala Arg 200 205 210 cgc atc gcc cac ctc acc tac cgt ggc gaa cta gaa atc gac gaa cgc 787 Arg Ile Ala His Leu Thr Tyr Arg Gly Glu Leu Glu Ile Asp Glu Arg 215 220 225 ttc ggc acc aaa gcc caa aag aac gaa aac cca ctc ggt ccc tac cgc 835 Phe Gly Thr Lys Ala Gln Lys Asn Glu Asn Pro Leu Gly Pro Tyr Arg 230 235 240 245 aag ccc gac cag cgc ttc gcc gtg gaa tcc tac ttg gac tac caa gca 883 Lys Pro Asp Gln Arg Phe Ala Val Glu Ser Tyr Leu Asp Tyr Gln Ala 250 255 260 gac aag cta gta cag cgt ttc gac gcc ggc tcc tac gtc ttg ctc acc 931 Asp Lys Leu Val Gln Arg Phe Asp Ala Gly Ser Tyr Val Leu Leu Thr 265 270 275 gac gcc ctc aac cgc cac gac att ggt cgc gac cgc gga ggc ctc aac 979 Asp Ala Leu Asn Arg His Asp Ile Gly Arg Asp Arg Gly Gly Leu Asn 280 285 290 aag gca ctc gaa tcc atc aaa gtt cca gtc ctt gtc gca ggc gta gat 1027 Lys Ala Leu Glu Ser Ile Lys Val Pro Val Leu Val Ala Gly Val Asp 295 300 305 acc gat att ttg tac ccc tac cac cag caa gaa cac ctc tcc aga aac 1075 Thr Asp Ile Leu Tyr Pro Tyr His Gln Gln Glu His Leu Ser Arg Asn 310 315 320 325 ctg gga aat cta ctg gca atg gca aaa atc gta tcc cct gtc ggc cac 1123 Leu Gly Asn Leu Leu Ala Met Ala Lys Ile Val Ser Pro Val Gly His 330 335 340 gat gct ttc ctc acc gaa agc cgc caa atg gat cgc atc gtg agg aac 1171 Asp Ala Phe Leu Thr Glu Ser Arg Gln Met Asp Arg Ile Val Arg Asn 345 350 355 ttc ttc agc ctc atc tcc cca gac gaa gac aac cct tcg 1210 Phe Phe Ser Leu Ile Ser Pro Asp Glu Asp Asn Pro Ser 360 365 370 74 370 PRT Corynebacterium glutamicum 74 Met Pro Thr Leu Ala Pro Ser Gly Gln Leu Glu Ile Gln Ala Ile Gly 1 5 10 15 Asp Val Ser Thr Glu Ala Gly Ala Ile Ile Thr Asn Ala Glu Ile Ala 20 25 30 Tyr His Arg Trp Gly Glu Tyr Arg Val Asp Lys Glu Gly Arg Ser Asn 35 40 45 Val Val Leu Ile Glu His Ala Leu Thr Gly Asp Ser Asn Ala Ala Asp 50 55 60 Trp Trp Ala Asp Leu Leu Gly Pro Gly Lys Ala Ile Asn Thr Asp Ile 65 70 75 80 Tyr Cys Val Ile Cys Thr Asn Val Ile Gly Gly Cys Asn Gly Ser Thr 85 90 95 Gly Pro Gly Ser Met His Pro Asp Gly Asn Phe Trp Gly Asn Arg Phe 100 105 110 Pro Ala Thr Ser Ile Arg Asp Gln Val Asn Ala Glu Lys Gln Phe Leu 115 120 125 Asp Ala Leu Gly Ile Thr Thr Val Ala Ala Val Leu Gly Gly Ser Met 130 135 140 Gly Gly Ala Arg Thr Leu Glu Trp Ala Ala Met Tyr Pro Glu Thr Val 145 150 155 160 Gly Ala Ala Ala Val Leu Ala Val Ser Ala Arg Ala Ser Ala Trp Gln 165 170 175 Ile Gly Ile Gln Ser Ala Gln Ile Lys Ala Ile Glu Asn Asp His His 180 185 190 Trp His Glu Gly Asn Tyr Tyr Glu Ser Gly Cys Asn Pro Ala Thr Gly 195 200 205 Leu Gly Ala Ala Arg Arg Ile Ala His Leu Thr Tyr Arg Gly Glu Leu 210 215 220 Glu Ile Asp Glu Arg Phe Gly Thr Lys Ala Gln Lys Asn Glu Asn Pro 225 230 235 240 Leu Gly Pro Tyr Arg Lys Pro Asp Gln Arg Phe Ala Val Glu Ser Tyr 245 250 255 Leu Asp Tyr Gln Ala Asp Lys Leu Val Gln Arg Phe Asp Ala Gly Ser 260 265 270 Tyr Val Leu Leu Thr Asp Ala Leu Asn Arg His Asp Ile Gly Arg Asp 275 280 285 Arg Gly Gly Leu Asn Lys Ala Leu Glu Ser Ile Lys Val Pro Val Leu 290 295 300 Val Ala Gly Val Asp Thr Asp Ile Leu Tyr Pro Tyr His Gln Gln Glu 305 310 315 320 His Leu Ser Arg Asn Leu Gly Asn Leu Leu Ala Met Ala Lys Ile Val 325 330 335 Ser Pro Val Gly His Asp Ala Phe Leu Thr Glu Ser Arg Gln Met Asp 340 345 350 Arg Ile Val Arg Asn Phe Phe Ser Leu Ile Ser Pro Asp Glu Asp Asn 355 360 365 Pro Ser 370 75 687 DNA Corynebacterium glutamicum CDS (101)..(664) RXS03158 75 caaagctcac cgaaggcacc aacgccaagt tggttgttga caacaccttg gcatccccat 60 acctgcagca gccactaaaa ctcggcgcac acgcaagtcc ttg cac tcc acc acc 115 Leu His Ser Thr Thr 1 5 aag tac atc gaa gga cac tcc gac gtt gtt ggc ggc ctt gtg ggt acc 163 Lys Tyr Ile Glu Gly His Ser Asp Val Val Gly Gly Leu Val Gly Thr 10 15 20 aac gac cag gaa atg gac gaa gaa ctg ctg ttc atg cag ggc ggc atc 211 Asn Asp Gln Glu Met Asp Glu Glu Leu Leu Phe Met Gln Gly Gly Ile 25 30 35 gga ccg atc cca tca gtt ttc gat gca tac ctg acc gcc cgt ggc ctc 259 Gly Pro Ile Pro Ser Val Phe Asp Ala Tyr Leu Thr Ala Arg Gly Leu 40 45 50 aag acc ctt gca gtg cgc atg gat cgc cac tgc gac aac gca gaa aag 307 Lys Thr Leu Ala Val Arg Met Asp Arg His Cys Asp Asn Ala Glu Lys 55 60 65 atc gcg gaa ttc ctg gac tcc cgc cca gag gtc tcc acc gtg ctc tac 355 Ile Ala Glu Phe Leu Asp Ser Arg Pro Glu Val Ser Thr Val Leu Tyr 70 75 80 85 cca ggt ctg aag aac cac cca ggc cac gaa gtc gca gcg aag cag atg 403 Pro Gly Leu Lys Asn His Pro Gly His Glu Val Ala Ala Lys Gln Met 90 95 100 aag cgc ttc ggc ggc atg atc tcc gtc cgt ttc gca ggc ggc gaa gaa 451 Lys Arg Phe Gly Gly Met Ile Ser Val Arg Phe Ala Gly Gly Glu Glu 105 110 115 gca gct aag aag ttc tgt acc tcc acc aaa ctg atc tgt ctg gcc gag 499 Ala Ala Lys Lys Phe Cys Thr Ser Thr Lys Leu Ile Cys Leu Ala Glu 120 125 130 tcc ctc ggt ggc gtg gaa tcc ctc ctg gag cac cca gca acc atg acc 547 Ser Leu Gly Gly Val Glu Ser Leu Leu Glu His Pro Ala Thr Met Thr 135 140 145 cac cag tca gct gcc ggc tct cag ctc gag gtt ccc cgc gac ctc gtg 595 His Gln Ser Ala Ala Gly Ser Gln Leu Glu Val Pro Arg Asp Leu Val 150 155 160 165 cgc atc tcc att ggt att gaa gac att gaa gac ctg ctc gca gat gtc 643 Arg Ile Ser Ile Gly Ile Glu Asp Ile Glu Asp Leu Leu Ala Asp Val 170 175 180 gag cag gcc ctc aat aac ctt tagaaactat ttggcggcaa gca 687 Glu Gln Ala Leu Asn Asn Leu 185 76 188 PRT Corynebacterium glutamicum 76 Leu His Ser Thr Thr Lys Tyr Ile Glu Gly His Ser Asp Val Val Gly 1 5 10 15 Gly Leu Val Gly Thr Asn Asp Gln Glu Met Asp Glu Glu Leu Leu Phe 20 25 30 Met Gln Gly Gly Ile Gly Pro Ile Pro Ser Val Phe Asp Ala Tyr Leu 35 40 45 Thr Ala Arg Gly Leu Lys Thr Leu Ala Val Arg Met Asp Arg His Cys 50 55 60 Asp Asn Ala Glu Lys Ile Ala Glu Phe Leu Asp Ser Arg Pro Glu Val 65 70 75 80 Ser Thr Val Leu Tyr Pro Gly Leu Lys Asn His Pro Gly His Glu Val 85 90 95 Ala Ala Lys Gln Met Lys Arg Phe Gly Gly Met Ile Ser Val Arg Phe 100 105 110 Ala Gly Gly Glu Glu Ala Ala Lys Lys Phe Cys Thr Ser Thr Lys Leu 115 120 125 Ile Cys Leu Ala Glu Ser Leu Gly Gly Val Glu Ser Leu Leu Glu His 130 135 140 Pro Ala Thr Met Thr His Gln Ser Ala Ala Gly Ser Gln Leu Glu Val 145 150 155 160 Pro Arg Asp Leu Val Arg Ile Ser Ile Gly Ile Glu Asp Ile Glu Asp 165 170 175 Leu Leu Ala Asp Val Glu Gln Ala Leu Asn Asn Leu 180 185 77 617 DNA Corynebacterium glutamicum CDS (1)..(594) FRXA00254 77 cag cca cta aaa ctc ggc gca cac gca gtc ttg cac tcc acc acc aag 48 Gln Pro Leu Lys Leu Gly Ala His Ala Val Leu His Ser Thr Thr Lys 1 5 10 15 tac atc gga gga cac tcc gac gtt gtt ggc ggc ctt gtg gtt acc aac 96 Tyr Ile Gly Gly His Ser Asp Val Val Gly Gly Leu Val Val Thr Asn 20 25 30 gac cag gaa atg gac gaa gaa ctg ctg ttc atg cag ggc ggc atc gga 144 Asp Gln Glu Met Asp Glu Glu Leu Leu Phe Met Gln Gly Gly Ile Gly 35 40 45 ccg atc cca tca gtt ttc gat gca tac ctg acc gcc cgt ggc ctc aag 192 Pro Ile Pro Ser Val Phe Asp Ala Tyr Leu Thr Ala Arg Gly Leu Lys 50 55 60 acc ctt gca gtg cgc atg gat cgc cac tgc gac aac gca gaa aag atc 240 Thr Leu Ala Val Arg Met Asp Arg His Cys Asp Asn Ala Glu Lys Ile 65 70 75 80 gcg gaa ttc ctg gac tcc cgc cca gag gtc tcc acc gtg ctc tac cca 288 Ala Glu Phe Leu Asp Ser Arg Pro Glu Val Ser Thr Val Leu Tyr Pro 85 90 95 ggt ctg aag aac cac cca ggc cac gaa gtc gca gcg aag cag atg aag 336 Gly Leu Lys Asn His Pro Gly His Glu Val Ala Ala Lys Gln Met Lys 100 105 110 cgc ttc ggc ggc atg atc tcc gtc cgt ttc gca ggc ggc gaa gaa gca 384 Arg Phe Gly Gly Met Ile Ser Val Arg Phe Ala Gly Gly Glu Glu Ala 115 120 125 gct aag aag ttc tgt acc tcc acc aaa ctg atc tgt ctg gcc gag tcc 432 Ala Lys Lys Phe Cys Thr Ser Thr Lys Leu Ile Cys Leu Ala Glu Ser 130 135 140 ctc ggt ggc gtg gaa tcc ctc ctg gag cac cca gca acc atg acc cac 480 Leu Gly Gly Val Glu Ser Leu Leu Glu His Pro Ala Thr Met Thr His 145 150 155 160 cag tca gct gcc ggc tct cag ctc gag gtt ccc cgc gac ctc gtg cgc 528 Gln Ser Ala Ala Gly Ser Gln Leu Glu Val Pro Arg Asp Leu Val Arg 165 170 175 atc tcc att ggt att gaa gac att gaa gac ctg ctc gca gat gtc gag 576 Ile Ser Ile Gly Ile Glu Asp Ile Glu Asp Leu Leu Ala Asp Val Glu 180 185 190 cag gcc ctc aat aac ctt tagaaactat ttggcggcaa gca 617 Gln Ala Leu Asn Asn Leu 195 78 198 PRT Corynebacterium glutamicum 78 Gln Pro Leu Lys Leu Gly Ala His Ala Val Leu His Ser Thr Thr Lys 1 5 10 15 Tyr Ile Gly Gly His Ser Asp Val Val Gly Gly Leu Val Val Thr Asn 20 25 30 Asp Gln Glu Met Asp Glu Glu Leu Leu Phe Met Gln Gly Gly Ile Gly 35 40 45 Pro Ile Pro Ser Val Phe Asp Ala Tyr Leu Thr Ala Arg Gly Leu Lys 50 55 60 Thr Leu Ala Val Arg Met Asp Arg His Cys Asp Asn Ala Glu Lys Ile 65 70 75 80 Ala Glu Phe Leu Asp Ser Arg Pro Glu Val Ser Thr Val Leu Tyr Pro 85 90 95 Gly Leu Lys Asn His Pro Gly His Glu Val Ala Ala Lys Gln Met Lys 100 105 110 Arg Phe Gly Gly Met Ile Ser Val Arg Phe Ala Gly Gly Glu Glu Ala 115 120 125 Ala Lys Lys Phe Cys Thr Ser Thr Lys Leu Ile Cys Leu Ala Glu Ser 130 135 140 Leu Gly Gly Val Glu Ser Leu Leu Glu His Pro Ala Thr Met Thr His 145 150 155 160 Gln Ser Ala Ala Gly Ser Gln Leu Glu Val Pro Arg Asp Leu Val Arg 165 170 175 Ile Ser Ile Gly Ile Glu Asp Ile Glu Asp Leu Leu Ala Asp Val Glu 180 185 190 Gln Ala Leu Asn Asn Leu 195 79 1170 DNA Corynebacterium glutamicum CDS (101)..(1147) RXA02532 79 gatgaatttt tacccaccat ctgtacctat taaccctgcg tggcgtccac ccacagtaac 60 tgtgcaagcg ggacggccag ccagaactcc tggtgcgccg atg aac cca cct atc 115 Met Asn Pro Pro Ile 1 5 acg ttg tcc agc act tat gtt cat gat tca gaa aaa gct tat ggg cgc 163 Thr Leu Ser Ser Thr Tyr Val His Asp Ser Glu Lys Ala Tyr Gly Arg 10 15 20 gat ggc aat gat gga tgg ggt gca ttt gag gct gcc atg gga act cta 211 Asp Gly Asn Asp Gly Trp Gly Ala Phe Glu Ala Ala Met Gly Thr Leu 25 30 35 gat ggt ggg ttc gcg gta tct tat tct tca ggt ttg gca gcg gca acg 259 Asp Gly Gly Phe Ala Val Ser Tyr Ser Ser Gly Leu Ala Ala Ala Thr 40 45 50 tcg att gct gat ttg gtt cct act ggt ggc aca gtt gtt tta cct aaa 307 Ser Ile Ala Asp Leu Val Pro Thr Gly Gly Thr Val Val Leu Pro Lys 55 60 65 gct gcc tat tat ggc gtg acc aat att ttc gcc agg atg gaa gcc cgc 355 Ala Ala Tyr Tyr Gly Val Thr Asn Ile Phe Ala Arg Met Glu Ala Arg 70 75 80 85 gga agg ctg aag gtt cga act gtt gat gca gac aat acc gaa gaa gtg 403 Gly Arg Leu Lys Val Arg Thr Val Asp Ala Asp Asn Thr Glu Glu Val 90 95 100 att gct gct gct caa ggt gca gat gtg gtg tgg gtg gaa tcg atc gct 451 Ile Ala Ala Ala Gln Gly Ala Asp Val Val Trp Val Glu Ser Ile Ala 105 110 115 aat ccg acg atg gtg gta gct gat atc cct gca ata gtc gac ggt gtg 499 Asn Pro Thr Met Val Val Ala Asp Ile Pro Ala Ile Val Asp Gly Val 120 125 130 cgt ggg ctt gga gtt ttg act gtc gtt gac gcg act ttc gca acg cca 547 Arg Gly Leu Gly Val Leu Thr Val Val Asp Ala Thr Phe Ala Thr Pro 135 140 145 ctt cgt caa cgt cca ttg gaa ctt ggt gct gat att gtg ctt tac tcg 595 Leu Arg Gln Arg Pro Leu Glu Leu Gly Ala Asp Ile Val Leu Tyr Ser 150 155 160 165 gca acc aaa ctt atc ggt gga cac tct gat ctt ctt ctt gga gtc gca 643 Ala Thr Lys Leu Ile Gly Gly His Ser Asp Leu Leu Leu Gly Val Ala 170 175 180 gtg tgc aag tct gag cac cat gcg cag ttt ctt gcc act cac cgt cat 691 Val Cys Lys Ser Glu His His Ala Gln Phe Leu Ala Thr His Arg His 185 190 195 gat cat ggt tca gtg ccg gga ggt ctt gaa gcg ttt ctt gct ctc cgt 739 Asp His Gly Ser Val Pro Gly Gly Leu Glu Ala Phe Leu Ala Leu Arg 200 205 210 gga ttg tat tcc ttg gcg gtg cgt ctt gat cga gca gaa tcc aac gca 787 Gly Leu Tyr Ser Leu Ala Val Arg Leu Asp Arg Ala Glu Ser Asn Ala 215 220 225 gca gaa ctt tcg cgg cga ctt aac gcg cat cct tcg gtt acc cgc gtc 835 Ala Glu Leu Ser Arg Arg Leu Asn Ala His Pro Ser Val Thr Arg Val 230 235 240 245 aat tat cca gga ctt cct gat gat ccc caa cat gaa aaa gcc gtg cga 883 Asn Tyr Pro Gly Leu Pro Asp Asp Pro Gln His Glu Lys Ala Val Arg 250 255 260 gtc cta ccc tct gga tgt gga aac atg ttg tca ttt gag ctt gat gca 931 Val Leu Pro Ser Gly Cys Gly Asn Met Leu Ser Phe Glu Leu Asp Ala 265 270 275 aca cct gaa cga act gat gag att ctc gaa agc ctg tca ctt tta acc 979 Thr Pro Glu Arg Thr Asp Glu Ile Leu Glu Ser Leu Ser Leu Leu Thr 280 285 290 cac gcg acc agt tgg gga ggt gtg gaa aca gcc att gaa cgt cgc acc 1027 His Ala Thr Ser Trp Gly Gly Val Glu Thr Ala Ile Glu Arg Arg Thr 295 300 305 agg cgg gat gct gaa gtg gtg gca gaa gta ccg atg act ctt tgc cgc 1075 Arg Arg Asp Ala Glu Val Val Ala Glu Val Pro Met Thr Leu Cys Arg 310 315 320 325 gtt tcc gta gga att gaa gac gtt gaa gat cta tgg gaa gac ctc aac 1123 Val Ser Val Gly Ile Glu Asp Val Glu Asp Leu Trp Glu Asp Leu Asn 330 335 340 gcc tca atc gac aaa gtt ctg ggt tagaactcgt agccagtaac cag 1170 Ala Ser Ile Asp Lys Val Leu Gly 345 80 349 PRT Corynebacterium glutamicum 80 Met Asn Pro Pro Ile Thr Leu Ser Ser Thr Tyr Val His Asp Ser Glu 1 5 10 15 Lys Ala Tyr Gly Arg Asp Gly Asn Asp Gly Trp Gly Ala Phe Glu Ala 20 25 30 Ala Met Gly Thr Leu Asp Gly Gly Phe Ala Val Ser Tyr Ser Ser Gly 35 40 45 Leu Ala Ala Ala Thr Ser Ile Ala Asp Leu Val Pro Thr Gly Gly Thr 50 55 60 Val Val Leu Pro Lys Ala Ala Tyr Tyr Gly Val Thr Asn Ile Phe Ala 65 70 75 80 Arg Met Glu Ala Arg Gly Arg Leu Lys Val Arg Thr Val Asp Ala Asp 85 90 95 Asn Thr Glu Glu Val Ile Ala Ala Ala Gln Gly Ala Asp Val Val Trp 100 105 110 Val Glu Ser Ile Ala Asn Pro Thr Met Val Val Ala Asp Ile Pro Ala 115 120 125 Ile Val Asp Gly Val Arg Gly Leu Gly Val Leu Thr Val Val Asp Ala 130 135 140 Thr Phe Ala Thr Pro Leu Arg Gln Arg Pro Leu Glu Leu Gly Ala Asp 145 150 155 160 Ile Val Leu Tyr Ser Ala Thr Lys Leu Ile Gly Gly His Ser Asp Leu 165 170 175 Leu Leu Gly Val Ala Val Cys Lys Ser Glu His His Ala Gln Phe Leu 180 185 190 Ala Thr His Arg His Asp His Gly Ser Val Pro Gly Gly Leu Glu Ala 195 200 205 Phe Leu Ala Leu Arg Gly Leu Tyr Ser Leu Ala Val Arg Leu Asp Arg 210 215 220 Ala Glu Ser Asn Ala Ala Glu Leu Ser Arg Arg Leu Asn Ala His Pro 225 230 235 240 Ser Val Thr Arg Val Asn Tyr Pro Gly Leu Pro Asp Asp Pro Gln His 245 250 255 Glu Lys Ala Val Arg Val Leu Pro Ser Gly Cys Gly Asn Met Leu Ser 260 265 270 Phe Glu Leu Asp Ala Thr Pro Glu Arg Thr Asp Glu Ile Leu Glu Ser 275 280 285 Leu Ser Leu Leu Thr His Ala Thr Ser Trp Gly Gly Val Glu Thr Ala 290 295 300 Ile Glu Arg Arg Thr Arg Arg Asp Ala Glu Val Val Ala Glu Val Pro 305 310 315 320 Met Thr Leu Cys Arg Val Ser Val Gly Ile Glu Asp Val Glu Asp Leu 325 330 335 Trp Glu Asp Leu Asn Ala Ser Ile Asp Lys Val Leu Gly 340 345 81 861 DNA Corynebacterium glutamicum CDS (101)..(838) RXS03159 81 aggggctagt tttacacaaa agtggacagc ttggtctatc attgccagaa gaccggtcct 60 tttagggcca tagaattctg attacaggag ttgatctacc ttg tct ttt gac cca 115 Leu Ser Phe Asp Pro 1 5 aac acc cag ggt ttc tcc act gca tcg att cac gct ggg tat gag cca 163 Asn Thr Gln Gly Phe Ser Thr Ala Ser Ile His Ala Gly Tyr Glu Pro 10 15 20 gac gac tac tac ggt tcg att aac acc cca atc tat gcc tcc acc acc 211 Asp Asp Tyr Tyr Gly Ser Ile Asn Thr Pro Ile Tyr Ala Ser Thr Thr 25 30 35 ttc gcg cag aac gct cca aac gaa ctg cgc aaa ggc tac gag tac acc 259 Phe Ala Gln Asn Ala Pro Asn Glu Leu Arg Lys Gly Tyr Glu Tyr Thr 40 45 50 cgt gtg ggc aac ccc acc atc gtg gca tta gag cag acc gtc gca gca 307 Arg Val Gly Asn Pro Thr Ile Val Ala Leu Glu Gln Thr Val Ala Ala 55 60 65 ctc gaa ggc gca aag tat ggc cgc gca ttc tcc tcc ggc atg gct gca 355 Leu Glu Gly Ala Lys Tyr Gly Arg Ala Phe Ser Ser Gly Met Ala Ala 70 75 80 85 acc gac atc ctg ttc cgc atc atc ctc aag ccg ggc gat cac atc gtc 403 Thr Asp Ile Leu Phe Arg Ile Ile Leu Lys Pro Gly Asp His Ile Val 90 95 100 ctc ggc aac gat gct tac ggc gga acc tac cgc ctg atc gac acc gta 451 Leu Gly Asn Asp Ala Tyr Gly Gly Thr Tyr Arg Leu Ile Asp Thr Val 105 110 115 ttc acc gca tgg ggc gtc gaa tac acc gtt gtt gat acc tcc gtc gtg 499 Phe Thr Ala Trp Gly Val Glu Tyr Thr Val Val Asp Thr Ser Val Val 120 125 130 gaa gag gtc aag gca gcg atc aag gac aac acc aag ctg atc tgg gtg 547 Glu Glu Val Lys Ala Ala Ile Lys Asp Asn Thr Lys Leu Ile Trp Val 135 140 145 gaa acc cca acc aac cca gca ctt ggc atc acc gac atc gaa gca gta 595 Glu Thr Pro Thr Asn Pro Ala Leu Gly Ile Thr Asp Ile Glu Ala Val 150 155 160 165 gca aag ctc acc gaa ggc acc aac gcc aag ttg gtt gtt gac aac acc 643 Ala Lys Leu Thr Glu Gly Thr Asn Ala Lys Leu Val Val Asp Asn Thr 170 175 180 ttg gca tcc cca tac ctg cag cag cca cta aaa ctc ggc gca cac gca 691 Leu Ala Ser Pro Tyr Leu Gln Gln Pro Leu Lys Leu Gly Ala His Ala 185 190 195 agt cct tgc act cca cca cca agt aca tcg aag gac act ccg acg ttg 739 Ser Pro Cys Thr Pro Pro Pro Ser Thr Ser Lys Asp Thr Pro Thr Leu 200 205 210 ttg gcg gcc ttg tgg gta cca acg acc agg aaa tgg acg aag aac tgc 787 Leu Ala Ala Leu Trp Val Pro Thr Thr Arg Lys Trp Thr Lys Asn Cys 215 220 225 tgt tca tgc agg gcg gca tcg gac cga tcc cat cag ttt tcg atg cat 835 Cys Ser Cys Arg Ala Ala Ser Asp Arg Ser His Gln Phe Ser Met His 230 235 240 245 acc tgaccgcccg tggcctcaag acc 861 Thr 82 246 PRT Corynebacterium glutamicum 82 Leu Ser Phe Asp Pro Asn Thr Gln Gly Phe Ser Thr Ala Ser Ile His 1 5 10 15 Ala Gly Tyr Glu Pro Asp Asp Tyr Tyr Gly Ser Ile Asn Thr Pro Ile 20 25 30 Tyr Ala Ser Thr Thr Phe Ala Gln Asn Ala Pro Asn Glu Leu Arg Lys 35 40 45 Gly Tyr Glu Tyr Thr Arg Val Gly Asn Pro Thr Ile Val Ala Leu Glu 50 55 60 Gln Thr Val Ala Ala Leu Glu Gly Ala Lys Tyr Gly Arg Ala Phe Ser 65 70 75 80 Ser Gly Met Ala Ala Thr Asp Ile Leu Phe Arg Ile Ile Leu Lys Pro 85 90 95 Gly Asp His Ile Val Leu Gly Asn Asp Ala Tyr Gly Gly Thr Tyr Arg 100 105 110 Leu Ile Asp Thr Val Phe Thr Ala Trp Gly Val Glu Tyr Thr Val Val 115 120 125 Asp Thr Ser Val Val Glu Glu Val Lys Ala Ala Ile Lys Asp Asn Thr 130 135 140 Lys Leu Ile Trp Val Glu Thr Pro Thr Asn Pro Ala Leu Gly Ile Thr 145 150 155 160 Asp Ile Glu Ala Val Ala Lys Leu Thr Glu Gly Thr Asn Ala Lys Leu 165 170 175 Val Val Asp Asn Thr Leu Ala Ser Pro Tyr Leu Gln Gln Pro Leu Lys 180 185 190 Leu Gly Ala His Ala Ser Pro Cys Thr Pro Pro Pro Ser Thr Ser Lys 195 200 205 Asp Thr Pro Thr Leu Leu Ala Ala Leu Trp Val Pro Thr Thr Arg Lys 210 215 220 Trp Thr Lys Asn Cys Cys Ser Cys Arg Ala Ala Ser Asp Arg Ser His 225 230 235 240 Gln Phe Ser Met His Thr 245 83 703 DNA Corynebacterium glutamicum CDS (101)..(703) FRXA02768 83 aggggctagt tttacacaaa agtggacagc ttggtctatc attgccagaa gaccggtcct 60 tttagggcca tagaattctg attacaggag ttgatctacc ttg tct ttt gac cca 115 Leu Ser Phe Asp Pro 1 5 aac acc cag ggt ttc tcc act gca tcg att cac gct ggg tat gag cca 163 Asn Thr Gln Gly Phe Ser Thr Ala Ser Ile His Ala Gly Tyr Glu Pro 10 15 20 gac gac tac tac ggt tcg att aac acc cca atc tat gcc tcc acc acc 211 Asp Asp Tyr Tyr Gly Ser Ile Asn Thr Pro Ile Tyr Ala Ser Thr Thr 25 30 35 ttc gcg cag aac gct cca aac gaa ctg cgc aaa ggc tac gag tac acc 259 Phe Ala Gln Asn Ala Pro Asn Glu Leu Arg Lys Gly Tyr Glu Tyr Thr 40 45 50 cgt gtg ggc aac ccc acc atc gtg gca tta gag cag acc gtc gca gca 307 Arg Val Gly Asn Pro Thr Ile Val Ala Leu Glu Gln Thr Val Ala Ala 55 60 65 ctc gaa ggc gca aag tat ggc cgc gca ttc tcc tcc ggc atg gct gca 355 Leu Glu Gly Ala Lys Tyr Gly Arg Ala Phe Ser Ser Gly Met Ala Ala 70 75 80 85 acc gac atc ctg ttc cgc atc atc ctc aag ccg ggc gat cac atc gtc 403 Thr Asp Ile Leu Phe Arg Ile Ile Leu Lys Pro Gly Asp His Ile Val 90 95 100 ctc ggc aac gat gct tac ggc gga acc tac cgc ctg atc gac acc gta 451 Leu Gly Asn Asp Ala Tyr Gly Gly Thr Tyr Arg Leu Ile Asp Thr Val 105 110 115 ttc acc gca tgg ggc gtc gaa tac acc gtt gtt gat acc tcc gtc gtg 499 Phe Thr Ala Trp Gly Val Glu Tyr Thr Val Val Asp Thr Ser Val Val 120 125 130 gaa gag gtc aag gca gcg atc aag gac aac acc aag gct gat ctt ggt 547 Glu Glu Val Lys Ala Ala Ile Lys Asp Asn Thr Lys Ala Asp Leu Gly 135 140 145 gga aac ccc aac caa ccc agc act ttg gca tta ccc gac atc gaa gca 595 Gly Asn Pro Asn Gln Pro Ser Thr Leu Ala Leu Pro Asp Ile Glu Ala 150 155 160 165 gtn tgc aaa act tca ccc gaa agg cac caa ccc caa gct tgt tgt ttg 643 Val Cys Lys Thr Ser Pro Glu Arg His Gln Pro Gln Ala Cys Cys Leu 170 175 180 aca aca cct tcg cat tcc cca tac ctg cag can cca ctt aaa ant tnn 691 Thr Thr Pro Ser His Ser Pro Tyr Leu Gln Xaa Pro Leu Lys Xaa Xaa 185 190 195 gng cac acg cag 703 Xaa His Thr Gln 200 84 201 PRT Corynebacterium glutamicum VARIANT 192 Xaa = His or Gln 84 Leu Ser Phe Asp Pro Asn Thr Gln Gly Phe Ser Thr Ala Ser Ile His 1 5 10 15 Ala Gly Tyr Glu Pro Asp Asp Tyr Tyr Gly Ser Ile Asn Thr Pro Ile 20 25 30 Tyr Ala Ser Thr Thr Phe Ala Gln Asn Ala Pro Asn Glu Leu Arg Lys 35 40 45 Gly Tyr Glu Tyr Thr Arg Val Gly Asn Pro Thr Ile Val Ala Leu Glu 50 55 60 Gln Thr Val Ala Ala Leu Glu Gly Ala Lys Tyr Gly Arg Ala Phe Ser 65 70 75 80 Ser Gly Met Ala Ala Thr Asp Ile Leu Phe Arg Ile Ile Leu Lys Pro 85 90 95 Gly Asp His Ile Val Leu Gly Asn Asp Ala Tyr Gly Gly Thr Tyr Arg 100 105 110 Leu Ile Asp Thr Val Phe Thr Ala Trp Gly Val Glu Tyr Thr Val Val 115 120 125 Asp Thr Ser Val Val Glu Glu Val Lys Ala Ala Ile Lys Asp Asn Thr 130 135 140 Lys Ala Asp Leu Gly Gly Asn Pro Asn Gln Pro Ser Thr Leu Ala Leu 145 150 155 160 Pro Asp Ile Glu Ala Val Cys Lys Thr Ser Pro Glu Arg His Gln Pro 165 170 175 Gln Ala Cys Cys Leu Thr Thr Pro Ser His Ser Pro Tyr Leu Gln Xaa 180 185 190 Pro Leu Lys Xaa Xaa Xaa His Thr Gln 195 200 85 1113 DNA Corynebacterium glutamicum CDS (101)..(1090) RXA00216 85 gtgttgctcg cggccaggca gcagtgctgt acctgcctga cgcggatggt gacatcgttc 60 ttggatcagg caccatctgc cacacggagt cttaagaaaa ttg ggc gct tat ggt 115 Leu Gly Ala Tyr Gly 1 5 tta ggt gag ctt cct gga aaa tcc gcc gcg gaa gcc gcc gac att att 163 Leu Gly Glu Leu Pro Gly Lys Ser Ala Ala Glu Ala Ala Asp Ile Ile 10 15 20 cag ggt gaa acg ggc gat ctt ctc cat att cct cag ctt ccg gcg cga 211 Gln Gly Glu Thr Gly Asp Leu Leu His Ile Pro Gln Leu Pro Ala Arg 25 30 35 ggt ttg ggt gct gat ctg atc ggt cga acc gtc ggt ctg ctg gac atg 259 Gly Leu Gly Ala Asp Leu Ile Gly Arg Thr Val Gly Leu Leu Asp Met 40 45 50 atc aac gtt gat cgc ggg gcc cga tct tgg gtg atg agc aca cgc ccc 307 Ile Asn Val Asp Arg Gly Ala Arg Ser Trp Val Met Ser Thr Arg Pro 55 60 65 agc aga ttg acg cac ctg acc ggc gat ttc ctt gac atg gat ttg gat 355 Ser Arg Leu Thr His Leu Thr Gly Asp Phe Leu Asp Met Asp Leu Asp 70 75 80 85 gcg tgc gag gaa acc tgg gga acg ggc gtc gac aag cta aaa atc caa 403 Ala Cys Glu Glu Thr Trp Gly Thr Gly Val Asp Lys Leu Lys Ile Gln 90 95 100 gtt gct ggt ccc tgg act tta ggt gcg cgc att gag ttg gcc aat ggc 451 Val Ala Gly Pro Trp Thr Leu Gly Ala Arg Ile Glu Leu Ala Asn Gly 105 110 115 cat cgc gtt ttg tct gat cgc ggt gcg atg cgt gat ctc acg cag gcg 499 His Arg Val Leu Ser Asp Arg Gly Ala Met Arg Asp Leu Thr Gln Ala 120 125 130 ctg atc gcc ggc atc gat gcg cat gca cgc aag gtt gct ggg cga ttt 547 Leu Ile Ala Gly Ile Asp Ala His Ala Arg Lys Val Ala Gly Arg Phe 135 140 145 cgc gcc gaa gtg cag gtg caa att gat gag ccg gag ctg aaa tcg ctt 595 Arg Ala Glu Val Gln Val Gln Ile Asp Glu Pro Glu Leu Lys Ser Leu 150 155 160 165 atc gac ggc tcc ctc cct ggc act tcc acc ttt gac att att cct gcg 643 Ile Asp Gly Ser Leu Pro Gly Thr Ser Thr Phe Asp Ile Ile Pro Ala 170 175 180 gtg aat gtc gct gat gcc agt gaa cgt ttg cag cag gtc ttt agc tcg 691 Val Asn Val Ala Asp Ala Ser Glu Arg Leu Gln Gln Val Phe Ser Ser 185 190 195 att gag ggg ccg aca tat ctc aac ctc acc ggc cag att cct act tgg 739 Ile Glu Gly Pro Thr Tyr Leu Asn Leu Thr Gly Gln Ile Pro Thr Trp 200 205 210 gat gtg gct cgg ggt gcg ggc gcc gat act gtg cag att tcc atg gat 787 Asp Val Ala Arg Gly Ala Gly Ala Asp Thr Val Gln Ile Ser Met Asp 215 220 225 caa gtc cgt gga aat gaa cat ttg gat ggt ttt ggt gaa acc atc acc 835 Gln Val Arg Gly Asn Glu His Leu Asp Gly Phe Gly Glu Thr Ile Thr 230 235 240 245 agt gga att cgt ctt ggt ttg ggc att acg aca gga aaa gat gtc gta 883 Ser Gly Ile Arg Leu Gly Leu Gly Ile Thr Thr Gly Lys Asp Val Val 250 255 260 gat gaa ctg ctc gag cga ccg cgg caa aag gcc gtt gag gta gca cgc 931 Asp Glu Leu Leu Glu Arg Pro Arg Gln Lys Ala Val Glu Val Ala Arg 265 270 275 ttt ttt gat cgt tta ggt gtg ggc cga aac tat ctc gtg gat gct gtt 979 Phe Phe Asp Arg Leu Gly Val Gly Arg Asn Tyr Leu Val Asp Ala Val 280 285 290 gat att cat ccg ggt gag gat ttg gtg cag ggg acc atc acc gag gcc 1027 Asp Ile His Pro Gly Glu Asp Leu Val Gln Gly Thr Ile Thr Glu Ala 295 300 305 gcg cag gct tat cgc atg gcc cgg gtg atg tcg gag atg ttg tcg aag 1075 Ala Gln Ala Tyr Arg Met Ala Arg Val Met Ser Glu Met Leu Ser Lys 310 315 320 325 gat tca tgc gac ctt taaggcttta ccggcgctgg gtg 1113 Asp Ser Cys Asp Leu 330 86 330 PRT Corynebacterium glutamicum 86 Leu Gly Ala Tyr Gly Leu Gly Glu Leu Pro Gly Lys Ser Ala Ala Glu 1 5 10 15 Ala Ala Asp Ile Ile Gln Gly Glu Thr Gly Asp Leu Leu His Ile Pro 20 25 30 Gln Leu Pro Ala Arg Gly Leu Gly Ala Asp Leu Ile Gly Arg Thr Val 35 40 45 Gly Leu Leu Asp Met Ile Asn Val Asp Arg Gly Ala Arg Ser Trp Val 50 55 60 Met Ser Thr Arg Pro Ser Arg Leu Thr His Leu Thr Gly Asp Phe Leu 65 70 75 80 Asp Met Asp Leu Asp Ala Cys Glu Glu Thr Trp Gly Thr Gly Val Asp 85 90 95 Lys Leu Lys Ile Gln Val Ala Gly Pro Trp Thr Leu Gly Ala Arg Ile 100 105 110 Glu Leu Ala Asn Gly His Arg Val Leu Ser Asp Arg Gly Ala Met Arg 115 120 125 Asp Leu Thr Gln Ala Leu Ile Ala Gly Ile Asp Ala His Ala Arg Lys 130 135 140 Val Ala Gly Arg Phe Arg Ala Glu Val Gln Val Gln Ile Asp Glu Pro 145 150 155 160 Glu Leu Lys Ser Leu Ile Asp Gly Ser Leu Pro Gly Thr Ser Thr Phe 165 170 175 Asp Ile Ile Pro Ala Val Asn Val Ala Asp Ala Ser Glu Arg Leu Gln 180 185 190 Gln Val Phe Ser Ser Ile Glu Gly Pro Thr Tyr Leu Asn Leu Thr Gly 195 200 205 Gln Ile Pro Thr Trp Asp Val Ala Arg Gly Ala Gly Ala Asp Thr Val 210 215 220 Gln Ile Ser Met Asp Gln Val Arg Gly Asn Glu His Leu Asp Gly Phe 225 230 235 240 Gly Glu Thr Ile Thr Ser Gly Ile Arg Leu Gly Leu Gly Ile Thr Thr 245 250 255 Gly Lys Asp Val Val Asp Glu Leu Leu Glu Arg Pro Arg Gln Lys Ala 260 265 270 Val Glu Val Ala Arg Phe Phe Asp Arg Leu Gly Val Gly Arg Asn Tyr 275 280 285 Leu Val Asp Ala Val Asp Ile His Pro Gly Glu Asp Leu Val Gln Gly 290 295 300 Thr Ile Thr Glu Ala Ala Gln Ala Tyr Arg Met Ala Arg Val Met Ser 305 310 315 320 Glu Met Leu Ser Lys Asp Ser Cys Asp Leu 325 330 87 551 DNA Corynebacterium glutamicum CDS (1)..(528) RXA02197 87 gcc gaa cgc atg cgc ttt agc ttc cca cgc cag cag cgc ggc agg ttc 48 Ala Glu Arg Met Arg Phe Ser Phe Pro Arg Gln Gln Arg Gly Arg Phe 1 5 10 15 ttg tgc atc gcg gat ttc att cgc cca cgc gag caa gct gtc aag gac 96 Leu Cys Ile Ala Asp Phe Ile Arg Pro Arg Glu Gln Ala Val Lys Asp 20 25 30 ggc caa gtg gac gtc atg cca ttc cag ctg gtc acc atg ggt aat cct 144 Gly Gln Val Asp Val Met Pro Phe Gln Leu Val Thr Met Gly Asn Pro 35 40 45 att gct gat ttc gcc aac gag ttg ttc gca gcc aat gaa tac cgc gag 192 Ile Ala Asp Phe Ala Asn Glu Leu Phe Ala Ala Asn Glu Tyr Arg Glu 50 55 60 tac ttg gaa gtt cac ggc atc ggc gtg cag ctc acc gaa gca ttg gcc 240 Tyr Leu Glu Val His Gly Ile Gly Val Gln Leu Thr Glu Ala Leu Ala 65 70 75 80 gag tac tgg cac tcc cga gtg cgc agc gaa ctc aag ctg aac gac ggt 288 Glu Tyr Trp His Ser Arg Val Arg Ser Glu Leu Lys Leu Asn Asp Gly 85 90 95 gga tct gtc gct gat ttt gat cca gaa gac aag acc aag ttc ttc gac 336 Gly Ser Val Ala Asp Phe Asp Pro Glu Asp Lys Thr Lys Phe Phe Asp 100 105 110 ctg gat tac cgc ggc gcc cgc ttc tcc ttt ggt tac ggt tct tgc cct 384 Leu Asp Tyr Arg Gly Ala Arg Phe Ser Phe Gly Tyr Gly Ser Cys Pro 115 120 125 gat ctg gaa gac cgc gca aag ctg gtg gaa ttg ctc gag cca ggc cgt 432 Asp Leu Glu Asp Arg Ala Lys Leu Val Glu Leu Leu Glu Pro Gly Arg 130 135 140 atc ggc gtg gag ttg tcc gag gaa ctc cag ctg cac cca gag cag tcc 480 Ile Gly Val Glu Leu Ser Glu Glu Leu Gln Leu His Pro Glu Gln Ser 145 150 155 160 aca gac gcg ttt gtg ctc tac cac cca gag gca aag tac ttt aac gtc 528 Thr Asp Ala Phe Val Leu Tyr His Pro Glu Ala Lys Tyr Phe Asn Val 165 170 175 taacaccttt gagagggaaa act 551 88 176 PRT Corynebacterium glutamicum 88 Ala Glu Arg Met Arg Phe Ser Phe Pro Arg Gln Gln Arg Gly Arg Phe 1 5 10 15 Leu Cys Ile Ala Asp Phe Ile Arg Pro Arg Glu Gln Ala Val Lys Asp 20 25 30 Gly Gln Val Asp Val Met Pro Phe Gln Leu Val Thr Met Gly Asn Pro 35 40 45 Ile Ala Asp Phe Ala Asn Glu Leu Phe Ala Ala Asn Glu Tyr Arg Glu 50 55 60 Tyr Leu Glu Val His Gly Ile Gly Val Gln Leu Thr Glu Ala Leu Ala 65 70 75 80 Glu Tyr Trp His Ser Arg Val Arg Ser Glu Leu Lys Leu Asn Asp Gly 85 90 95 Gly Ser Val Ala Asp Phe Asp Pro Glu Asp Lys Thr Lys Phe Phe Asp 100 105 110 Leu Asp Tyr Arg Gly Ala Arg Phe Ser Phe Gly Tyr Gly Ser Cys Pro 115 120 125 Asp Leu Glu Asp Arg Ala Lys Leu Val Glu Leu Leu Glu Pro Gly Arg 130 135 140 Ile Gly Val Glu Leu Ser Glu Glu Leu Gln Leu His Pro Glu Gln Ser 145 150 155 160 Thr Asp Ala Phe Val Leu Tyr His Pro Glu Ala Lys Tyr Phe Asn Val 165 170 175 89 2599 DNA Corynebacterium glutamicum CDS (101)..(2599) RXN02198 89 agactagtgg cgctttgcct gtgttgctta ggcggcgttg aaaatgaact acgaatgaaa 60 agttcgggaa ttgtctaatc cgtactaagc tgtctacaca atg tct act tca gtt 115 Met Ser Thr Ser Val 1 5 act tca cca gcc cac aac aac gca cat tcc tcc gaa ttt ttg gat gcg 163 Thr Ser Pro Ala His Asn Asn Ala His Ser Ser Glu Phe Leu Asp Ala 10 15 20 ttg gca aac cat gtg ttg atc ggc gac ggc gcc atg ggc acc cag ctc 211 Leu Ala Asn His Val Leu Ile Gly Asp Gly Ala Met Gly Thr Gln Leu 25 30 35 caa ggc ttt gac ctg gac gtg gaa aag gat ttc ctt gat ctg gag ggg 259 Gln Gly Phe Asp Leu Asp Val Glu Lys Asp Phe Leu Asp Leu Glu Gly 40 45 50 tgt aat gag att ctc aac gac acc cgc cct gat gtg ttg agg cag att 307 Cys Asn Glu Ile Leu Asn Asp Thr Arg Pro Asp Val Leu Arg Gln Ile 55 60 65 cac cgc gcc tac ttt gag gcg gga gct gac ttg gtt gag acc aat act 355 His Arg Ala Tyr Phe Glu Ala Gly Ala Asp Leu Val Glu Thr Asn Thr 70 75 80 85 ttt ggt tgc aac ctg ccg aac ttg gcg gat tat gac atc gct gat cgt 403 Phe Gly Cys Asn Leu Pro Asn Leu Ala Asp Tyr Asp Ile Ala Asp Arg 90 95 100 tgc cgt gag ctt gcc tac aag ggc act gca gtg gct agg gaa gtg gct 451 Cys Arg Glu Leu Ala Tyr Lys Gly Thr Ala Val Ala Arg Glu Val Ala 105 110 115 gat gag atg ggg ccg ggc cga aac ggc atg cgg cgt ttc gtg gtt ggt 499 Asp Glu Met Gly Pro Gly Arg Asn Gly Met Arg Arg Phe Val Val Gly 120 125 130 tcc ctg gga cct gga acg aag ctt cca tcg ctg ggc cat gca ccg tat 547 Ser Leu Gly Pro Gly Thr Lys Leu Pro Ser Leu Gly His Ala Pro Tyr 135 140 145 gca gat ttg cgt ggg cac tac aag gaa gca gcg ctt ggc atc atc gac 595 Ala Asp Leu Arg Gly His Tyr Lys Glu Ala Ala Leu Gly Ile Ile Asp 150 155 160 165 ggt ggt ggc gat gcc ttt ttg att gag act gct cag gac ttg ctt cag 643 Gly Gly Gly Asp Ala Phe Leu Ile Glu Thr Ala Gln Asp Leu Leu Gln 170 175 180 gtc aag gct gcg gtt cac ggc gtt caa gat gcc atg gct gaa ctt gat 691 Val Lys Ala Ala Val His Gly Val Gln Asp Ala Met Ala Glu Leu Asp 185 190 195 aca ttc ttg ccc att att tgc cac gtc acc gta gag acc acc ggc acc 739 Thr Phe Leu Pro Ile Ile Cys His Val Thr Val Glu Thr Thr Gly Thr 200 205 210 atg ctc atg ggt tct gag atc ggt gcc gcg ttg aca gcg ctg cag cca 787 Met Leu Met Gly Ser Glu Ile Gly Ala Ala Leu Thr Ala Leu Gln Pro 215 220 225 ctg ggt atc gac atg att ggt ctg aac tgc gcc acc ggc cca gat gag 835 Leu Gly Ile Asp Met Ile Gly Leu Asn Cys Ala Thr Gly Pro Asp Glu 230 235 240 245 atg agc gag cac ctg cgt tac ctg tcc aag cac gcc gat att cct gtg 883 Met Ser Glu His Leu Arg Tyr Leu Ser Lys His Ala Asp Ile Pro Val 250 255 260 tcg gtg atg cct aac gca ggt ctt cct gtc ctg ggt aaa aac ggt gca 931 Ser Val Met Pro Asn Ala Gly Leu Pro Val Leu Gly Lys Asn Gly Ala 265 270 275 gaa tac cca ctt gag gct gag gat ttg gcg cag gcg ctg gct gga ttc 979 Glu Tyr Pro Leu Glu Ala Glu Asp Leu Ala Gln Ala Leu Ala Gly Phe 280 285 290 gtc tcc gaa tat ggc ctg tcc atg gtg ggt ggt tgt tgt ggc acc aca 1027 Val Ser Glu Tyr Gly Leu Ser Met Val Gly Gly Cys Cys Gly Thr Thr 295 300 305 cct gag cac atc cgt gcg gtc cgc gat gcg gtg gtt ggt gtt cca gag 1075 Pro Glu His Ile Arg Ala Val Arg Asp Ala Val Val Gly Val Pro Glu 310 315 320 325 cag gaa acc tcc aca ctg acc aag atc cct gca ggc cct gtt gag cag 1123 Gln Glu Thr Ser Thr Leu Thr Lys Ile Pro Ala Gly Pro Val Glu Gln 330 335 340 gcc tcc cgc gag gtg gag aaa gag gac tcc gtc gcg tcg ctg tac acc 1171 Ala Ser Arg Glu Val Glu Lys Glu Asp Ser Val Ala Ser Leu Tyr Thr 345 350 355 tcg gtg cca ttg tcc cag gaa acc ggc att tcc atg atc ggt gag cgc 1219 Ser Val Pro Leu Ser Gln Glu Thr Gly Ile Ser Met Ile Gly Glu Arg 360 365 370 acc aac tcc aac ggt tcc aag gca ttc cgt gag gca atg ctg tct ggc 1267 Thr Asn Ser Asn Gly Ser Lys Ala Phe Arg Glu Ala Met Leu Ser Gly 375 380 385 gat tgg gaa aag tgt gtg gat att gcc aag cag caa acc cgc gat ggt 1315 Asp Trp Glu Lys Cys Val Asp Ile Ala Lys Gln Gln Thr Arg Asp Gly 390 395 400 405 gca cac atg ctg gat ctt tgt gtg gat tac gtg gga cga gac ggc acc 1363 Ala His Met Leu Asp Leu Cys Val Asp Tyr Val Gly Arg Asp Gly Thr 410 415 420 gcc gat atg gcg acc ttg gca gca ctt ctt gct acc agc tcc act ttg 1411 Ala Asp Met Ala Thr Leu Ala Ala Leu Leu Ala Thr Ser Ser Thr Leu 425 430 435 cca atc atg att gac tcc acc gag cca gag gtt att cgc aca ggc ctt 1459 Pro Ile Met Ile Asp Ser Thr Glu Pro Glu Val Ile Arg Thr Gly Leu 440 445 450 gag cac ttg ggt gga cga agc atc gtt aac tcc gtc aac ttt gaa gac 1507 Glu His Leu Gly Gly Arg Ser Ile Val Asn Ser Val Asn Phe Glu Asp 455 460 465 ggc gat ggc cct gag tcc cgc tac cag cgc atc atg aaa ctg gta aag 1555 Gly Asp Gly Pro Glu Ser Arg Tyr Gln Arg Ile Met Lys Leu Val Lys 470 475 480 485 cag cac ggt gcg gcc gtg gtt gcg ctg acc att gat gag gaa ggc cag 1603 Gln His Gly Ala Ala Val Val Ala Leu Thr Ile Asp Glu Glu Gly Gln 490 495 500 gca cgt acc gct gag cac aag gtg cgc att gct aaa cga ctg att gac 1651 Ala Arg Thr Ala Glu His Lys Val Arg Ile Ala Lys Arg Leu Ile Asp 505 510 515 gat atc acc ggc agc tac ggc ctg gat atc aaa gac atc gtt gtg gac 1699 Asp Ile Thr Gly Ser Tyr Gly Leu Asp Ile Lys Asp Ile Val Val Asp 520 525 530 tgc ctg acc ttc ccg atc tct act ggc cag gaa gaa acc agg cga gat 1747 Cys Leu Thr Phe Pro Ile Ser Thr Gly Gln Glu Glu Thr Arg Arg Asp 535 540 545 ggc att gaa acc atc gaa gcc atc cgc gag ctg aag aag ctc tac cca 1795 Gly Ile Glu Thr Ile Glu Ala Ile Arg Glu Leu Lys Lys Leu Tyr Pro 550 555 560 565 gaa atc cac acc acc ctg ggt ctg tcc aat att tcc ttc ggc ctg aac 1843 Glu Ile His Thr Thr Leu Gly Leu Ser Asn Ile Ser Phe Gly Leu Asn 570 575 580 cct gct gca cgc cag gtt ctt aac tct gtg ttc ctc aat gag tgc att 1891 Pro Ala Ala Arg Gln Val Leu Asn Ser Val Phe Leu Asn Glu Cys Ile 585 590 595 gag gct ggt ctg gac tct gcg att gcg cac agc tcc aag att ttg ccg 1939 Glu Ala Gly Leu Asp Ser Ala Ile Ala His Ser Ser Lys Ile Leu Pro 600 605 610 atg aac cgc att gat gat cgc cag cgc gaa gtg gcg ttg gat atg gtc 1987 Met Asn Arg Ile Asp Asp Arg Gln Arg Glu Val Ala Leu Asp Met Val 615 620 625 tat gat cgc cgc acc gag gat tac gat ccg ctg cag gaa ttc atg cag 2035 Tyr Asp Arg Arg Thr Glu Asp Tyr Asp Pro Leu Gln Glu Phe Met Gln 630 635 640 645 ctg ttt gag ggc gtt tct gct gcc gat gcc aag gat gct cgc gct gaa 2083 Leu Phe Glu Gly Val Ser Ala Ala Asp Ala Lys Asp Ala Arg Ala Glu 650 655 660 cag ctg gcc gct atg cct ttg ttt gag cgt ttg gca cag cgc atc atc 2131 Gln Leu Ala Ala Met Pro Leu Phe Glu Arg Leu Ala Gln Arg Ile Ile 665 670 675 gac ggc gat aag aat ggc ctt gag gat gat ctg gaa gca ggc atg aag 2179 Asp Gly Asp Lys Asn Gly Leu Glu Asp Asp Leu Glu Ala Gly Met Lys 680 685 690 gag aag tct cct att gcg atc atc aac gag gac ctt ctc aac ggc atg 2227 Glu Lys Ser Pro Ile Ala Ile Ile Asn Glu Asp Leu Leu Asn Gly Met 695 700 705 aag acc gtg ggt gag ctg ttt ggt tcc gga cag atg cag ctg cca ttc 2275 Lys Thr Val Gly Glu Leu Phe Gly Ser Gly Gln Met Gln Leu Pro Phe 710 715 720 725 gtg ctg caa tcg gca gaa acc atg aaa act gcg gtg gcc tat ttg gaa 2323 Val Leu Gln Ser Ala Glu Thr Met Lys Thr Ala Val Ala Tyr Leu Glu 730 735 740 ccg ttc atg gaa gag gaa gca gaa gct acc gga tct gcg cag gca gag 2371 Pro Phe Met Glu Glu Glu Ala Glu Ala Thr Gly Ser Ala Gln Ala Glu 745 750 755 ggc aag ggc aaa atc gtc gtg gcc acc gtc aag ggt gac gtg cac gat 2419 Gly Lys Gly Lys Ile Val Val Ala Thr Val Lys Gly Asp Val His Asp 760 765 770 atc ggc aag aac ttg gtg gac atc att ttg tcc aac aac ggt tac gac 2467 Ile Gly Lys Asn Leu Val Asp Ile Ile Leu Ser Asn Asn Gly Tyr Asp 775 780 785 gtg gtg aac ttg ggc atc aag cag cca ctg tcc gcc atg ttg gaa gca 2515 Val Val Asn Leu Gly Ile Lys Gln Pro Leu Ser Ala Met Leu Glu Ala 790 795 800 805 gcg gaa gaa cac aaa gca gac gtc atc ggc atg tcg gga ctt ctt gtg 2563 Ala Glu Glu His Lys Ala Asp Val Ile Gly Met Ser Gly Leu Leu Val 810 815 820 aag tcc acc gtg gtg atg aag caa acc atc agc gac 2599 Lys Ser Thr Val Val Met Lys Gln Thr Ile Ser Asp 825 830 90 833 PRT Corynebacterium glutamicum 90 Met Ser Thr Ser Val Thr Ser Pro Ala His Asn Asn Ala His Ser Ser 1 5 10 15 Glu Phe Leu Asp Ala Leu Ala Asn His Val Leu Ile Gly Asp Gly Ala 20 25 30 Met Gly Thr Gln Leu Gln Gly Phe Asp Leu Asp Val Glu Lys Asp Phe 35 40 45 Leu Asp Leu Glu Gly Cys Asn Glu Ile Leu Asn Asp Thr Arg Pro Asp 50 55 60 Val Leu Arg Gln Ile His Arg Ala Tyr Phe Glu Ala Gly Ala Asp Leu 65 70 75 80 Val Glu Thr Asn Thr Phe Gly Cys Asn Leu Pro Asn Leu Ala Asp Tyr 85 90 95 Asp Ile Ala Asp Arg Cys Arg Glu Leu Ala Tyr Lys Gly Thr Ala Val 100 105 110 Ala Arg Glu Val Ala Asp Glu Met Gly Pro Gly Arg Asn Gly Met Arg 115 120 125 Arg Phe Val Val Gly Ser Leu Gly Pro Gly Thr Lys Leu Pro Ser Leu 130 135 140 Gly His Ala Pro Tyr Ala Asp Leu Arg Gly His Tyr Lys Glu Ala Ala 145 150 155 160 Leu Gly Ile Ile Asp Gly Gly Gly Asp Ala Phe Leu Ile Glu Thr Ala 165 170 175 Gln Asp Leu Leu Gln Val Lys Ala Ala Val His Gly Val Gln Asp Ala 180 185 190 Met Ala Glu Leu Asp Thr Phe Leu Pro Ile Ile Cys His Val Thr Val 195 200 205 Glu Thr Thr Gly Thr Met Leu Met Gly Ser Glu Ile Gly Ala Ala Leu 210 215 220 Thr Ala Leu Gln Pro Leu Gly Ile Asp Met Ile Gly Leu Asn Cys Ala 225 230 235 240 Thr Gly Pro Asp Glu Met Ser Glu His Leu Arg Tyr Leu Ser Lys His 245 250 255 Ala Asp Ile Pro Val Ser Val Met Pro Asn Ala Gly Leu Pro Val Leu 260 265 270 Gly Lys Asn Gly Ala Glu Tyr Pro Leu Glu Ala Glu Asp Leu Ala Gln 275 280 285 Ala Leu Ala Gly Phe Val Ser Glu Tyr Gly Leu Ser Met Val Gly Gly 290 295 300 Cys Cys Gly Thr Thr Pro Glu His Ile Arg Ala Val Arg Asp Ala Val 305 310 315 320 Val Gly Val Pro Glu Gln Glu Thr Ser Thr Leu Thr Lys Ile Pro Ala 325 330 335 Gly Pro Val Glu Gln Ala Ser Arg Glu Val Glu Lys Glu Asp Ser Val 340 345 350 Ala Ser Leu Tyr Thr Ser Val Pro Leu Ser Gln Glu Thr Gly Ile Ser 355 360 365 Met Ile Gly Glu Arg Thr Asn Ser Asn Gly Ser Lys Ala Phe Arg Glu 370 375 380 Ala Met Leu Ser Gly Asp Trp Glu Lys Cys Val Asp Ile Ala Lys Gln 385 390 395 400 Gln Thr Arg Asp Gly Ala His Met Leu Asp Leu Cys Val Asp Tyr Val 405 410 415 Gly Arg Asp Gly Thr Ala Asp Met Ala Thr Leu Ala Ala Leu Leu Ala 420 425 430 Thr Ser Ser Thr Leu Pro Ile Met Ile Asp Ser Thr Glu Pro Glu Val 435 440 445 Ile Arg Thr Gly Leu Glu His Leu Gly Gly Arg Ser Ile Val Asn Ser 450 455 460 Val Asn Phe Glu Asp Gly Asp Gly Pro Glu Ser Arg Tyr Gln Arg Ile 465 470 475 480 Met Lys Leu Val Lys Gln His Gly Ala Ala Val Val Ala Leu Thr Ile 485 490 495 Asp Glu Glu Gly Gln Ala Arg Thr Ala Glu His Lys Val Arg Ile Ala 500 505 510 Lys Arg Leu Ile Asp Asp Ile Thr Gly Ser Tyr Gly Leu Asp Ile Lys 515 520 525 Asp Ile Val Val Asp Cys Leu Thr Phe Pro Ile Ser Thr Gly Gln Glu 530 535 540 Glu Thr Arg Arg Asp Gly Ile Glu Thr Ile Glu Ala Ile Arg Glu Leu 545 550 555 560 Lys Lys Leu Tyr Pro Glu Ile His Thr Thr Leu Gly Leu Ser Asn Ile 565 570 575 Ser Phe Gly Leu Asn Pro Ala Ala Arg Gln Val Leu Asn Ser Val Phe 580 585 590 Leu Asn Glu Cys Ile Glu Ala Gly Leu Asp Ser Ala Ile Ala His Ser 595 600 605 Ser Lys Ile Leu Pro Met Asn Arg Ile Asp Asp Arg Gln Arg Glu Val 610 615 620 Ala Leu Asp Met Val Tyr Asp Arg Arg Thr Glu Asp Tyr Asp Pro Leu 625 630 635 640 Gln Glu Phe Met Gln Leu Phe Glu Gly Val Ser Ala Ala Asp Ala Lys 645 650 655 Asp Ala Arg Ala Glu Gln Leu Ala Ala Met Pro Leu Phe Glu Arg Leu 660 665 670 Ala Gln Arg Ile Ile Asp Gly Asp Lys Asn Gly Leu Glu Asp Asp Leu 675 680 685 Glu Ala Gly Met Lys Glu Lys Ser Pro Ile Ala Ile Ile Asn Glu Asp 690 695 700 Leu Leu Asn Gly Met Lys Thr Val Gly Glu Leu Phe Gly Ser Gly Gln 705 710 715 720 Met Gln Leu Pro Phe Val Leu Gln Ser Ala Glu Thr Met Lys Thr Ala 725 730 735 Val Ala Tyr Leu Glu Pro Phe Met Glu Glu Glu Ala Glu Ala Thr Gly 740 745 750 Ser Ala Gln Ala Glu Gly Lys Gly Lys Ile Val Val Ala Thr Val Lys 755 760 765 Gly Asp Val His Asp Ile Gly Lys Asn Leu Val Asp Ile Ile Leu Ser 770 775 780 Asn Asn Gly Tyr Asp Val Val Asn Leu Gly Ile Lys Gln Pro Leu Ser 785 790 795 800 Ala Met Leu Glu Ala Ala Glu Glu His Lys Ala Asp Val Ile Gly Met 805 810 815 Ser Gly Leu Leu Val Lys Ser Thr Val Val Met Lys Gln Thr Ile Ser 820 825 830 Asp 91 2578 DNA Corynebacterium glutamicum CDS (101)..(2578) FRXA02198 91 agactagtgg cgctttgcct gtgttgctta ggcggcgttg aaaatgaact acgaatgaaa 60 agttcgggaa ttgtctaatc cgtactaagc tgtctacaca atg tct act tca gtt 115 Met Ser Thr Ser Val 1 5 act tca cca gcc cac aac aac gca cat tcc tcc gaa ttt ttg gat gcg 163 Thr Ser Pro Ala His Asn Asn Ala His Ser Ser Glu Phe Leu Asp Ala 10 15 20 ttg gca aac cat gtg ttg atc ggc gac ggc gcc atg ggc acc cag ctc 211 Leu Ala Asn His Val Leu Ile Gly Asp Gly Ala Met Gly Thr Gln Leu 25 30 35 caa ggc ttt gac ctg gac gtg gaa aag gat ttc ctt gat ctg gag ggg 259 Gln Gly Phe Asp Leu Asp Val Glu Lys Asp Phe Leu Asp Leu Glu Gly 40 45 50 tgt aat gag att ctc aac gac acc cgc cct gat gtg ttg agg cag att 307 Cys Asn Glu Ile Leu Asn Asp Thr Arg Pro Asp Val Leu Arg Gln Ile 55 60 65 cac cgc gcc tac ttt gag gcg gga gct gac ttg gtt gag acc aat act 355 His Arg Ala Tyr Phe Glu Ala Gly Ala Asp Leu Val Glu Thr Asn Thr 70 75 80 85 ttt ggt tgc aac ctg ccg aac ttg gcg gat tat gac atc gct gat cgt 403 Phe Gly Cys Asn Leu Pro Asn Leu Ala Asp Tyr Asp Ile Ala Asp Arg 90 95 100 tgc cgt gag ctt gcc tac aag ggc act gca gtg gct agg gaa gtg gct 451 Cys Arg Glu Leu Ala Tyr Lys Gly Thr Ala Val Ala Arg Glu Val Ala 105 110 115 gat gag atg ggg ccg ggc cga aac ggc atg cgg cgt ttc gtg gtt ggt 499 Asp Glu Met Gly Pro Gly Arg Asn Gly Met Arg Arg Phe Val Val Gly 120 125 130 tcc ctg gga cct gga acg aag ctt cca tcg ctg ggc cat gca ccg tat 547 Ser Leu Gly Pro Gly Thr Lys Leu Pro Ser Leu Gly His Ala Pro Tyr 135 140 145 gca gat ttg cgt ggg cac tac aag gaa gca gcg ctt ggc atc atc gac 595 Ala Asp Leu Arg Gly His Tyr Lys Glu Ala Ala Leu Gly Ile Ile Asp 150 155 160 165 ggt ggt ggc gat gcc ttt ttg att gag act gct cag gac ttg ctt cag 643 Gly Gly Gly Asp Ala Phe Leu Ile Glu Thr Ala Gln Asp Leu Leu Gln 170 175 180 gtc aag gct gcg gtt cac ggc gtt caa gat gcc atg gct gaa ctt gat 691 Val Lys Ala Ala Val His Gly Val Gln Asp Ala Met Ala Glu Leu Asp 185 190 195 aca ttc ttg ccc att att tgc cac gtc acc gta gag acc acc ggc acc 739 Thr Phe Leu Pro Ile Ile Cys His Val Thr Val Glu Thr Thr Gly Thr 200 205 210 atg ctc atg ggt tct gag atc ggt gcc gcg ttg aca gcg ctg cag cca 787 Met Leu Met Gly Ser Glu Ile Gly Ala Ala Leu Thr Ala Leu Gln Pro 215 220 225 ctg ggt atc gac atg att ggt ctg aac tgc gcc acc ggc cca gat gag 835 Leu Gly Ile Asp Met Ile Gly Leu Asn Cys Ala Thr Gly Pro Asp Glu 230 235 240 245 atg agc gag cac ctg cgt tac ctg tcc aag cac gcc gat att cct gtg 883 Met Ser Glu His Leu Arg Tyr Leu Ser Lys His Ala Asp Ile Pro Val 250 255 260 tcg gtg atg cct aac gca ggt ctt cct gtc ctg ggt aaa aac ggt gca 931 Ser Val Met Pro Asn Ala Gly Leu Pro Val Leu Gly Lys Asn Gly Ala 265 270 275 gaa tac cca ctt gag gct gag gat ttg gcg cag gcg ctg gct gga ttc 979 Glu Tyr Pro Leu Glu Ala Glu Asp Leu Ala Gln Ala Leu Ala Gly Phe 280 285 290 gtc tcc gaa tat ggc ctg tcc atg gtg ggt ggt tgt tgt ggc acc aca 1027 Val Ser Glu Tyr Gly Leu Ser Met Val Gly Gly Cys Cys Gly Thr Thr 295 300 305 cct gag cac atc cgt gcg gtc cgc gat gcg gtg gtt ggt gtt cca gag 1075 Pro Glu His Ile Arg Ala Val Arg Asp Ala Val Val Gly Val Pro Glu 310 315 320 325 cag gaa acc tcc aca ctg acc aag atc cct gca ggc cct gtt gag cag 1123 Gln Glu Thr Ser Thr Leu Thr Lys Ile Pro Ala Gly Pro Val Glu Gln 330 335 340 gcc tcc cgc gag gtg gag aaa gag gac tcc gtc gcg tcg ctg tac acc 1171 Ala Ser Arg Glu Val Glu Lys Glu Asp Ser Val Ala Ser Leu Tyr Thr 345 350 355 tcg gtg cca ttg tcc cag gaa acc ggc att tcc atg atc ggt gag cgc 1219 Ser Val Pro Leu Ser Gln Glu Thr Gly Ile Ser Met Ile Gly Glu Arg 360 365 370 acc aac tcc aac ggt tcc aag gca ttc cgt gag gca atg ctg tct ggc 1267 Thr Asn Ser Asn Gly Ser Lys Ala Phe Arg Glu Ala Met Leu Ser Gly 375 380 385 gat tgg gaa aag tgt gtg gat att gcc aag cag caa acc cgc gat ggt 1315 Asp Trp Glu Lys Cys Val Asp Ile Ala Lys Gln Gln Thr Arg Asp Gly 390 395 400 405 gca cac atg ctg gat ctt tgt gtg gat tac gtg gga cga gac ggc acc 1363 Ala His Met Leu Asp Leu Cys Val Asp Tyr Val Gly Arg Asp Gly Thr 410 415 420 gcc gat atg gcg acc ttg gca gca ctt ctt gct acc agc tcc act ttg 1411 Ala Asp Met Ala Thr Leu Ala Ala Leu Leu Ala Thr Ser Ser Thr Leu 425 430 435 cca atc atg att gac tcc acc gag cca gag gtt att cgc aca ggc ctt 1459 Pro Ile Met Ile Asp Ser Thr Glu Pro Glu Val Ile Arg Thr Gly Leu 440 445 450 gag cac ttg ggt gga cga agc atc gtt aac tcc gtc aac ttt gaa gac 1507 Glu His Leu Gly Gly Arg Ser Ile Val Asn Ser Val Asn Phe Glu Asp 455 460 465 ggc gat ggc cct gag tcc cgc tac cag cgc atc atg aaa ctg gta aag 1555 Gly Asp Gly Pro Glu Ser Arg Tyr Gln Arg Ile Met Lys Leu Val Lys 470 475 480 485 cag cac ggt gcg gcc gtg gtt gcg ctg acc att gat gag gaa ggc cag 1603 Gln His Gly Ala Ala Val Val Ala Leu Thr Ile Asp Glu Glu Gly Gln 490 495 500 gca cgt acc gct gag cac aag gtg cgc att gct aaa cga ctg att gac 1651 Ala Arg Thr Ala Glu His Lys Val Arg Ile Ala Lys Arg Leu Ile Asp 505 510 515 gat atc acc ggc agc tac ggc ctg gat atc aaa gac atc gtt gtg gac 1699 Asp Ile Thr Gly Ser Tyr Gly Leu Asp Ile Lys Asp Ile Val Val Asp 520 525 530 tgc ctg acc ttc ccg atc tct act ggc cag gaa gaa acc agg cga gat 1747 Cys Leu Thr Phe Pro Ile Ser Thr Gly Gln Glu Glu Thr Arg Arg Asp 535 540 545 ggc att gaa acc atc gaa gcc atc cgc gag ctg aag aag ctc tac cca 1795 Gly Ile Glu Thr Ile Glu Ala Ile Arg Glu Leu Lys Lys Leu Tyr Pro 550 555 560 565 gaa atc cac acc acc ctg ggt ctg tcc aat att tcc ttc ggc ctg aac 1843 Glu Ile His Thr Thr Leu Gly Leu Ser Asn Ile Ser Phe Gly Leu Asn 570 575 580 cct gct gca cgc cag gtt ctt aac tct gtg ttc ctc aat gag tgc att 1891 Pro Ala Ala Arg Gln Val Leu Asn Ser Val Phe Leu Asn Glu Cys Ile 585 590 595 gag gct ggt ctg gac tct gcg att gcg cac agc tcc aag att ttg ccg 1939 Glu Ala Gly Leu Asp Ser Ala Ile Ala His Ser Ser Lys Ile Leu Pro 600 605 610 atg aac cgc att gat gat cgc cag cgc gaa gtg gcg ttg gat atg gtc 1987 Met Asn Arg Ile Asp Asp Arg Gln Arg Glu Val Ala Leu Asp Met Val 615 620 625 tat gat cgc cgc acc gag gat tac gat ccg ctg cag gaa ttc atg cag 2035 Tyr Asp Arg Arg Thr Glu Asp Tyr Asp Pro Leu Gln Glu Phe Met Gln 630 635 640 645 ctg ttt gag ggc gtt tct gct gcc gat gcc aag gat gct cgc gct gaa 2083 Leu Phe Glu Gly Val Ser Ala Ala Asp Ala Lys Asp Ala Arg Ala Glu 650 655 660 cag ctg gcc gct atg cct ttg ttt gag cgt ttg gca cag cgc atc atc 2131 Gln Leu Ala Ala Met Pro Leu Phe Glu Arg Leu Ala Gln Arg Ile Ile 665 670 675 gac ggc gat aag aat ggc ctt gag gat gat ctg gaa gca ggc atg aag 2179 Asp Gly Asp Lys Asn Gly Leu Glu Asp Asp Leu Glu Ala Gly Met Lys 680 685 690 gag aag tct cct att gcg atc atc aac gag gac ctt ctc aac ggc atg 2227 Glu Lys Ser Pro Ile Ala Ile Ile Asn Glu Asp Leu Leu Asn Gly Met 695 700 705 aag acc gtg ggt gag ctg ttt ggt tcc gga cag atg cag ctg cca ttc 2275 Lys Thr Val Gly Glu Leu Phe Gly Ser Gly Gln Met Gln Leu Pro Phe 710 715 720 725 gtg ctg caa tcg gca gaa acc atg aaa act gcg gtg gcc tat ttg gaa 2323 Val Leu Gln Ser Ala Glu Thr Met Lys Thr Ala Val Ala Tyr Leu Glu 730 735 740 ccg ttc atg gaa gag gaa gca gaa gct acc gga tct gcg cag gca gag 2371 Pro Phe Met Glu Glu Glu Ala Glu Ala Thr Gly Ser Ala Gln Ala Glu 745 750 755 ggc aag ggc aaa atc gtc gtg gcc acc gtc aag ggt gac gtg cac gat 2419 Gly Lys Gly Lys Ile Val Val Ala Thr Val Lys Gly Asp Val His Asp 760 765 770 atc ggc aag aac ttg gtg gac atc att ttg tcc aac aac ggt tac gac 2467 Ile Gly Lys Asn Leu Val Asp Ile Ile Leu Ser Asn Asn Gly Tyr Asp 775 780 785 gtg gtg aac ttg ggc atc aag cag cca ctg tcc gcc atg ttg gaa gca 2515 Val Val Asn Leu Gly Ile Lys Gln Pro Leu Ser Ala Met Leu Glu Ala 790 795 800 805 gcg gaa gaa cac aaa gca gac gtc atc ggc atg tcg gga ctt ctt gtg 2563 Ala Glu Glu His Lys Ala Asp Val Ile Gly Met Ser Gly Leu Leu Val 810 815 820 aag tcc acc gtg gtg 2578 Lys Ser Thr Val Val 825 92 826 PRT Corynebacterium glutamicum 92 Met Ser Thr Ser Val Thr Ser Pro Ala His Asn Asn Ala His Ser Ser 1 5 10 15 Glu Phe Leu Asp Ala Leu Ala Asn His Val Leu Ile Gly Asp Gly Ala 20 25 30 Met Gly Thr Gln Leu Gln Gly Phe Asp Leu Asp Val Glu Lys Asp Phe 35 40 45 Leu Asp Leu Glu Gly Cys Asn Glu Ile Leu Asn Asp Thr Arg Pro Asp 50 55 60 Val Leu Arg Gln Ile His Arg Ala Tyr Phe Glu Ala Gly Ala Asp Leu 65 70 75 80 Val Glu Thr Asn Thr Phe Gly Cys Asn Leu Pro Asn Leu Ala Asp Tyr 85 90 95 Asp Ile Ala Asp Arg Cys Arg Glu Leu Ala Tyr Lys Gly Thr Ala Val 100 105 110 Ala Arg Glu Val Ala Asp Glu Met Gly Pro Gly Arg Asn Gly Met Arg 115 120 125 Arg Phe Val Val Gly Ser Leu Gly Pro Gly Thr Lys Leu Pro Ser Leu 130 135 140 Gly His Ala Pro Tyr Ala Asp Leu Arg Gly His Tyr Lys Glu Ala Ala 145 150 155 160 Leu Gly Ile Ile Asp Gly Gly Gly Asp Ala Phe Leu Ile Glu Thr Ala 165 170 175 Gln Asp Leu Leu Gln Val Lys Ala Ala Val His Gly Val Gln Asp Ala 180 185 190 Met Ala Glu Leu Asp Thr Phe Leu Pro Ile Ile Cys His Val Thr Val 195 200 205 Glu Thr Thr Gly Thr Met Leu Met Gly Ser Glu Ile Gly Ala Ala Leu 210 215 220 Thr Ala Leu Gln Pro Leu Gly Ile Asp Met Ile Gly Leu Asn Cys Ala 225 230 235 240 Thr Gly Pro Asp Glu Met Ser Glu His Leu Arg Tyr Leu Ser Lys His 245 250 255 Ala Asp Ile Pro Val Ser Val Met Pro Asn Ala Gly Leu Pro Val Leu 260 265 270 Gly Lys Asn Gly Ala Glu Tyr Pro Leu Glu Ala Glu Asp Leu Ala Gln 275 280 285 Ala Leu Ala Gly Phe Val Ser Glu Tyr Gly Leu Ser Met Val Gly Gly 290 295 300 Cys Cys Gly Thr Thr Pro Glu His Ile Arg Ala Val Arg Asp Ala Val 305 310 315 320 Val Gly Val Pro Glu Gln Glu Thr Ser Thr Leu Thr Lys Ile Pro Ala 325 330 335 Gly Pro Val Glu Gln Ala Ser Arg Glu Val Glu Lys Glu Asp Ser Val 340 345 350 Ala Ser Leu Tyr Thr Ser Val Pro Leu Ser Gln Glu Thr Gly Ile Ser 355 360 365 Met Ile Gly Glu Arg Thr Asn Ser Asn Gly Ser Lys Ala Phe Arg Glu 370 375 380 Ala Met Leu Ser Gly Asp Trp Glu Lys Cys Val Asp Ile Ala Lys Gln 385 390 395 400 Gln Thr Arg Asp Gly Ala His Met Leu Asp Leu Cys Val Asp Tyr Val 405 410 415 Gly Arg Asp Gly Thr Ala Asp Met Ala Thr Leu Ala Ala Leu Leu Ala 420 425 430 Thr Ser Ser Thr Leu Pro Ile Met Ile Asp Ser Thr Glu Pro Glu Val 435 440 445 Ile Arg Thr Gly Leu Glu His Leu Gly Gly Arg Ser Ile Val Asn Ser 450 455 460 Val Asn Phe Glu Asp Gly Asp Gly Pro Glu Ser Arg Tyr Gln Arg Ile 465 470 475 480 Met Lys Leu Val Lys Gln His Gly Ala Ala Val Val Ala Leu Thr Ile 485 490 495 Asp Glu Glu Gly Gln Ala Arg Thr Ala Glu His Lys Val Arg Ile Ala 500 505 510 Lys Arg Leu Ile Asp Asp Ile Thr Gly Ser Tyr Gly Leu Asp Ile Lys 515 520 525 Asp Ile Val Val Asp Cys Leu Thr Phe Pro Ile Ser Thr Gly Gln Glu 530 535 540 Glu Thr Arg Arg Asp Gly Ile Glu Thr Ile Glu Ala Ile Arg Glu Leu 545 550 555 560 Lys Lys Leu Tyr Pro Glu Ile His Thr Thr Leu Gly Leu Ser Asn Ile 565 570 575 Ser Phe Gly Leu Asn Pro Ala Ala Arg Gln Val Leu Asn Ser Val Phe 580 585 590 Leu Asn Glu Cys Ile Glu Ala Gly Leu Asp Ser Ala Ile Ala His Ser 595 600 605 Ser Lys Ile Leu Pro Met Asn Arg Ile Asp Asp Arg Gln Arg Glu Val 610 615 620 Ala Leu Asp Met Val Tyr Asp Arg Arg Thr Glu Asp Tyr Asp Pro Leu 625 630 635 640 Gln Glu Phe Met Gln Leu Phe Glu Gly Val Ser Ala Ala Asp Ala Lys 645 650 655 Asp Ala Arg Ala Glu Gln Leu Ala Ala Met Pro Leu Phe Glu Arg Leu 660 665 670 Ala Gln Arg Ile Ile Asp Gly Asp Lys Asn Gly Leu Glu Asp Asp Leu 675 680 685 Glu Ala Gly Met Lys Glu Lys Ser Pro Ile Ala Ile Ile Asn Glu Asp 690 695 700 Leu Leu Asn Gly Met Lys Thr Val Gly Glu Leu Phe Gly Ser Gly Gln 705 710 715 720 Met Gln Leu Pro Phe Val Leu Gln Ser Ala Glu Thr Met Lys Thr Ala 725 730 735 Val Ala Tyr Leu Glu Pro Phe Met Glu Glu Glu Ala Glu Ala Thr Gly 740 745 750 Ser Ala Gln Ala Glu Gly Lys Gly Lys Ile Val Val Ala Thr Val Lys 755 760 765 Gly Asp Val His Asp Ile Gly Lys Asn Leu Val Asp Ile Ile Leu Ser 770 775 780 Asn Asn Gly Tyr Asp Val Val Asn Leu Gly Ile Lys Gln Pro Leu Ser 785 790 795 800 Ala Met Leu Glu Ala Ala Glu Glu His Lys Ala Asp Val Ile Gly Met 805 810 815 Ser Gly Leu Leu Val Lys Ser Thr Val Val 820 825 93 621 DNA Corynebacterium glutamicum CDS (101)..(598) RXN03074 93 tttgtgggca atctggtttt ttcgtaattg tgtgggatga atctcttaaa aattcacatt 60 tagcaggaca agcatactgt tttagttcta tgctgtgggc atg act caa agt gct 115 Met Thr Gln Ser Ala 1 5 cca gaa ttc att gcc acc gca gac ctc gta gac atc atc ggc gac aac 163 Pro Glu Phe Ile Ala Thr Ala Asp Leu Val Asp Ile Ile Gly Asp Asn 10 15 20 gcg caa tca tgc gac act cag ttt caa aac ctt gga ggt gcc aca gaa 211 Ala Gln Ser Cys Asp Thr Gln Phe Gln Asn Leu Gly Gly Ala Thr Glu 25 30 35 ttc cac gga ata ata acc acc gtg aaa tgc ttc caa gac aac gcc ctc 259 Phe His Gly Ile Ile Thr Thr Val Lys Cys Phe Gln Asp Asn Ala Leu 40 45 50 ctg aaa tcc atc ctg agc gag gat aat cct ggg gga gtg ctg gtt atc 307 Leu Lys Ser Ile Leu Ser Glu Asp Asn Pro Gly Gly Val Leu Val Ile 55 60 65 gat ggc gac gca tcc gtg cac acc gcg cta gtt ggc gac atc att gca 355 Asp Gly Asp Ala Ser Val His Thr Ala Leu Val Gly Asp Ile Ile Ala 70 75 80 85 gga ctt gga aaa gat cat ggt tgg tcc gga gta att gtc aac gga gca 403 Gly Leu Gly Lys Asp His Gly Trp Ser Gly Val Ile Val Asn Gly Ala 90 95 100 att cga gac tcc gca gtc atc ggc acc atg acc ttt ggt tgt aaa gcc 451 Ile Arg Asp Ser Ala Val Ile Gly Thr Met Thr Phe Gly Cys Lys Ala 105 110 115 ctt gga acc aac ccg cgg aaa tcc act aaa act ggt tcc ggc gaa cga 499 Leu Gly Thr Asn Pro Arg Lys Ser Thr Lys Thr Gly Ser Gly Glu Arg 120 125 130 gac gta gtg gta tcg att ggt ggc att gac ttc att cct ggt cat tac 547 Asp Val Val Val Ser Ile Gly Gly Ile Asp Phe Ile Pro Gly His Tyr 135 140 145 gtc tac gcg gac tct gac gga att atc gtc acc gag gcg cca att aag 595 Val Tyr Ala Asp Ser Asp Gly Ile Ile Val Thr Glu Ala Pro Ile Lys 150 155 160 165 cag taatttgttt tgacgacgca gta 621 Gln 94 166 PRT Corynebacterium glutamicum 94 Met Thr Gln Ser Ala Pro Glu Phe Ile Ala Thr Ala Asp Leu Val Asp 1 5 10 15 Ile Ile Gly Asp Asn Ala Gln Ser Cys Asp Thr Gln Phe Gln Asn Leu 20 25 30 Gly Gly Ala Thr Glu Phe His Gly Ile Ile Thr Thr Val Lys Cys Phe 35 40 45 Gln Asp Asn Ala Leu Leu Lys Ser Ile Leu Ser Glu Asp Asn Pro Gly 50 55 60 Gly Val Leu Val Ile Asp Gly Asp Ala Ser Val His Thr Ala Leu Val 65 70 75 80 Gly Asp Ile Ile Ala Gly Leu Gly Lys Asp His Gly Trp Ser Gly Val 85 90 95 Ile Val Asn Gly Ala Ile Arg Asp Ser Ala Val Ile Gly Thr Met Thr 100 105 110 Phe Gly Cys Lys Ala Leu Gly Thr Asn Pro Arg Lys Ser Thr Lys Thr 115 120 125 Gly Ser Gly Glu Arg Asp Val Val Val Ser Ile Gly Gly Ile Asp Phe 130 135 140 Ile Pro Gly His Tyr Val Tyr Ala Asp Ser Asp Gly Ile Ile Val Thr 145 150 155 160 Glu Ala Pro Ile Lys Gln 165 95 621 DNA Corynebacterium glutamicum CDS (101)..(598) FRXA02906 95 tttgtgggca atctggtttt ttcgtaattg tgtgggatga atctcttaaa aattcacatt 60 tagcaggaca agcatactgt tttagttcta tgctgtgggc atg act caa agt gct 115 Met Thr Gln Ser Ala 1 5 cca gaa ttc att gcc acc gca gac ctc gta gac atc atc ggc gac aac 163 Pro Glu Phe Ile Ala Thr Ala Asp Leu Val Asp Ile Ile Gly Asp Asn 10 15 20 gcg caa tca tgc gac act cag ttt caa aac ctt gga ggt gcc aca gaa 211 Ala Gln Ser Cys Asp Thr Gln Phe Gln Asn Leu Gly Gly Ala Thr Glu 25 30 35 ttc cac gga ata ata acc acc gtg aaa tgc ttc caa gac aac gcc ctc 259 Phe His Gly Ile Ile Thr Thr Val Lys Cys Phe Gln Asp Asn Ala Leu 40 45 50 ctg aaa tcc atc ctg agc gag gat aat cct ggg gga gtg ctg gtt atc 307 Leu Lys Ser Ile Leu Ser Glu Asp Asn Pro Gly Gly Val Leu Val Ile 55 60 65 gat ggc gac gca tcc gtg cac acc gcg cta gtt ggc gac atc att gca 355 Asp Gly Asp Ala Ser Val His Thr Ala Leu Val Gly Asp Ile Ile Ala 70 75 80 85 gga ctt gga aaa gat cat ggt tgg tcc gga gta att gtc aac gga gca 403 Gly Leu Gly Lys Asp His Gly Trp Ser Gly Val Ile Val Asn Gly Ala 90 95 100 att cga gac tcc gca gtc atc ggc acc atg acc ttt ggt tgt aaa gcc 451 Ile Arg Asp Ser Ala Val Ile Gly Thr Met Thr Phe Gly Cys Lys Ala 105 110 115 ctt gga acc aac ccg cgg aaa tcc act aaa act ggt tcc ggc gaa cga 499 Leu Gly Thr Asn Pro Arg Lys Ser Thr Lys Thr Gly Ser Gly Glu Arg 120 125 130 gac gta gtg gta tcg att ggt ggc att gac ttc att cct ggt cat tac 547 Asp Val Val Val Ser Ile Gly Gly Ile Asp Phe Ile Pro Gly His Tyr 135 140 145 gtc tac gcg gac tct gac gga att atc gtc acc gag gcg cca att aag 595 Val Tyr Ala Asp Ser Asp Gly Ile Ile Val Thr Glu Ala Pro Ile Lys 150 155 160 165 cag taatttgttt tgacgacgca gta 621 Gln 96 166 PRT Corynebacterium glutamicum 96 Met Thr Gln Ser Ala Pro Glu Phe Ile Ala Thr Ala Asp Leu Val Asp 1 5 10 15 Ile Ile Gly Asp Asn Ala Gln Ser Cys Asp Thr Gln Phe Gln Asn Leu 20 25 30 Gly Gly Ala Thr Glu Phe His Gly Ile Ile Thr Thr Val Lys Cys Phe 35 40 45 Gln Asp Asn Ala Leu Leu Lys Ser Ile Leu Ser Glu Asp Asn Pro Gly 50 55 60 Gly Val Leu Val Ile Asp Gly Asp Ala Ser Val His Thr Ala Leu Val 65 70 75 80 Gly Asp Ile Ile Ala Gly Leu Gly Lys Asp His Gly Trp Ser Gly Val 85 90 95 Ile Val Asn Gly Ala Ile Arg Asp Ser Ala Val Ile Gly Thr Met Thr 100 105 110 Phe Gly Cys Lys Ala Leu Gly Thr Asn Pro Arg Lys Ser Thr Lys Thr 115 120 125 Gly Ser Gly Glu Arg Asp Val Val Val Ser Ile Gly Gly Ile Asp Phe 130 135 140 Ile Pro Gly His Tyr Val Tyr Ala Asp Ser Asp Gly Ile Ile Val Thr 145 150 155 160 Glu Ala Pro Ile Lys Gln 165 97 1557 DNA Corynebacterium glutamicum CDS (101)..(1534) RXN00132 97 aacagcttca atcaattcgg tgtccactcc aacatgtaga gtggtgcgcg ttaaaaaagt 60 tttcctaatt ttcattttct taaaaggagc tcgccaggac atg gca cag gtt atg 115 Met Ala Gln Val Met 1 5 gac ttc aag gtt gcc gat ctt tca cta gca gag gca gga cgt cac cag 163 Asp Phe Lys Val Ala Asp Leu Ser Leu Ala Glu Ala Gly Arg His Gln 10 15 20 att cgt ctt gca gag tat gag atg cca ggt ctc atg cag ttg cgc aag 211 Ile Arg Leu Ala Glu Tyr Glu Met Pro Gly Leu Met Gln Leu Arg Lys 25 30 35 gaa ttc gca gac gag cag cct ttg aag ggc gcc cga att gct ggt tct 259 Glu Phe Ala Asp Glu Gln Pro Leu Lys Gly Ala Arg Ile Ala Gly Ser 40 45 50 atc cac atg acg gtc cag acc gcc gtg ctt att gag acc ctc act gct 307 Ile His Met Thr Val Gln Thr Ala Val Leu Ile Glu Thr Leu Thr Ala 55 60 65 ttg ggc gct gag gtt cgt tgg gct tcc tgc aac att ttc tcc acc cag 355 Leu Gly Ala Glu Val Arg Trp Ala Ser Cys Asn Ile Phe Ser Thr Gln 70 75 80 85 gat gag gct gca gcg gct atc gtt gtc ggc tcc ggc acc gtc gaa gag 403 Asp Glu Ala Ala Ala Ala Ile Val Val Gly Ser Gly Thr Val Glu Glu 90 95 100 cca gct ggt gtt cca gta ttc gcg tgg aag ggt gag tca ctg gag gag 451 Pro Ala Gly Val Pro Val Phe Ala Trp Lys Gly Glu Ser Leu Glu Glu 105 110 115 tac tgg tgg tgc atc aac cag atc ttc agc tgg ggc gat gag ctg cca 499 Tyr Trp Trp Cys Ile Asn Gln Ile Phe Ser Trp Gly Asp Glu Leu Pro 120 125 130 aac atg atc ctc gac gac ggc ggt gac gcc acc atg gct gtt att cgc 547 Asn Met Ile Leu Asp Asp Gly Gly Asp Ala Thr Met Ala Val Ile Arg 135 140 145 ggt cgc gaa tac gag cag gct ggt ctg gtt cca cca gca gag gcc aac 595 Gly Arg Glu Tyr Glu Gln Ala Gly Leu Val Pro Pro Ala Glu Ala Asn 150 155 160 165 gat tcc gat gag tac atc gca ttc ttg ggc atg ctg cgt gag gtt ctt 643 Asp Ser Asp Glu Tyr Ile Ala Phe Leu Gly Met Leu Arg Glu Val Leu 170 175 180 gct gca gag cct ggc aag tgg ggc aag atc gct gag gcc gtt aag ggt 691 Ala Ala Glu Pro Gly Lys Trp Gly Lys Ile Ala Glu Ala Val Lys Gly 185 190 195 gtc acc gag gaa acc acc acc ggt gtg cac cgc ctg tac cac ttc gct 739 Val Thr Glu Glu Thr Thr Thr Gly Val His Arg Leu Tyr His Phe Ala 200 205 210 gaa gaa ggc gtg ctg cct ttc cca gcg atg aac gtc aac gac gct gtc 787 Glu Glu Gly Val Leu Pro Phe Pro Ala Met Asn Val Asn Asp Ala Val 215 220 225 acc aag tcc aag ttt gat aac aag tac ggc acc cgc cac tcc ctg atc 835 Thr Lys Ser Lys Phe Asp Asn Lys Tyr Gly Thr Arg His Ser Leu Ile 230 235 240 245 gac ggc atc aac cgc gcc act gac atg ctc atg ggc ggc aag aac gtg 883 Asp Gly Ile Asn Arg Ala Thr Asp Met Leu Met Gly Gly Lys Asn Val 250 255 260 ctt gtc tgc ggt tac ggc gat gtc ggc aag ggc tgc gct gag gct ttc 931 Leu Val Cys Gly Tyr Gly Asp Val Gly Lys Gly Cys Ala Glu Ala Phe 265 270 275 gac ggc cag ggc gct cgc gtc aag gtc acc gaa gct gac cca atc aac 979 Asp Gly Gln Gly Ala Arg Val Lys Val Thr Glu Ala Asp Pro Ile Asn 280 285 290 gct ctt cag gct ctg atg gat ggc tac tct gtg gtc acc gtt gat gag 1027 Ala Leu Gln Ala Leu Met Asp Gly Tyr Ser Val Val Thr Val Asp Glu 295 300 305 gcc atc gag gac gcc gac atc gtg atc acc gcg acc ggc aac aag gac 1075 Ala Ile Glu Asp Ala Asp Ile Val Ile Thr Ala Thr Gly Asn Lys Asp 310 315 320 325 atc att tcc ttc gag cag atg ctc aag atg aag gat cac gct ctg ctg 1123 Ile Ile Ser Phe Glu Gln Met Leu Lys Met Lys Asp His Ala Leu Leu 330 335 340 ggc aac atc ggt cac ttt gat aat gag atc gat atg cat tcc ctg ttg 1171 Gly Asn Ile Gly His Phe Asp Asn Glu Ile Asp Met His Ser Leu Leu 345 350 355 cac cgc gac gac gtc acc cgc acc acg atc aag cca cag gtc gac gag 1219 His Arg Asp Asp Val Thr Arg Thr Thr Ile Lys Pro Gln Val Asp Glu 360 365 370 ttc acc ttc tcc acc ggt cgc tcc atc atc gtc ctg tcc gaa ggt cgc 1267 Phe Thr Phe Ser Thr Gly Arg Ser Ile Ile Val Leu Ser Glu Gly Arg 375 380 385 ctg ttg aac ctt ggc aac gcc acc gga cac cca tca ttt gtc atg tcc 1315 Leu Leu Asn Leu Gly Asn Ala Thr Gly His Pro Ser Phe Val Met Ser 390 395 400 405 aac tct ttc gcc gat cag acc att gcg cag atc gaa ctg ttc caa aac 1363 Asn Ser Phe Ala Asp Gln Thr Ile Ala Gln Ile Glu Leu Phe Gln Asn 410 415 420 gaa gga cag tac gag aac gag gtc tac cgt ctg cct aag gtt ctc gac 1411 Glu Gly Gln Tyr Glu Asn Glu Val Tyr Arg Leu Pro Lys Val Leu Asp 425 430 435 gaa aag gtg gca cgc atc cac gtt gag gct ctc ggc ggt cag ctc acc 1459 Glu Lys Val Ala Arg Ile His Val Glu Ala Leu Gly Gly Gln Leu Thr 440 445 450 gaa ctg acc aag gag cag gct gag tac atc ggc gtt gac gtt gca ggc 1507 Glu Leu Thr Lys Glu Gln Ala Glu Tyr Ile Gly Val Asp Val Ala Gly 455 460 465 cca ttc aag ccg gag cac tac cgc tac taatgattgt cagcattgag gga 1557 Pro Phe Lys Pro Glu His Tyr Arg Tyr 470 475 98 478 PRT Corynebacterium glutamicum 98 Met Ala Gln Val Met Asp Phe Lys Val Ala Asp Leu Ser Leu Ala Glu 1 5 10 15 Ala Gly Arg His Gln Ile Arg Leu Ala Glu Tyr Glu Met Pro Gly Leu 20 25 30 Met Gln Leu Arg Lys Glu Phe Ala Asp Glu Gln Pro Leu Lys Gly Ala 35 40 45 Arg Ile Ala Gly Ser Ile His Met Thr Val Gln Thr Ala Val Leu Ile 50 55 60 Glu Thr Leu Thr Ala Leu Gly Ala Glu Val Arg Trp Ala Ser Cys Asn 65 70 75 80 Ile Phe Ser Thr Gln Asp Glu Ala Ala Ala Ala Ile Val Val Gly Ser 85 90 95 Gly Thr Val Glu Glu Pro Ala Gly Val Pro Val Phe Ala Trp Lys Gly 100 105 110 Glu Ser Leu Glu Glu Tyr Trp Trp Cys Ile Asn Gln Ile Phe Ser Trp 115 120 125 Gly Asp Glu Leu Pro Asn Met Ile Leu Asp Asp Gly Gly Asp Ala Thr 130 135 140 Met Ala Val Ile Arg Gly Arg Glu Tyr Glu Gln Ala Gly Leu Val Pro 145 150 155 160 Pro Ala Glu Ala Asn Asp Ser Asp Glu Tyr Ile Ala Phe Leu Gly Met 165 170 175 Leu Arg Glu Val Leu Ala Ala Glu Pro Gly Lys Trp Gly Lys Ile Ala 180 185 190 Glu Ala Val Lys Gly Val Thr Glu Glu Thr Thr Thr Gly Val His Arg 195 200 205 Leu Tyr His Phe Ala Glu Glu Gly Val Leu Pro Phe Pro Ala Met Asn 210 215 220 Val Asn Asp Ala Val Thr Lys Ser Lys Phe Asp Asn Lys Tyr Gly Thr 225 230 235 240 Arg His Ser Leu Ile Asp Gly Ile Asn Arg Ala Thr Asp Met Leu Met 245 250 255 Gly Gly Lys Asn Val Leu Val Cys Gly Tyr Gly Asp Val Gly Lys Gly 260 265 270 Cys Ala Glu Ala Phe Asp Gly Gln Gly Ala Arg Val Lys Val Thr Glu 275 280 285 Ala Asp Pro Ile Asn Ala Leu Gln Ala Leu Met Asp Gly Tyr Ser Val 290 295 300 Val Thr Val Asp Glu Ala Ile Glu Asp Ala Asp Ile Val Ile Thr Ala 305 310 315 320 Thr Gly Asn Lys Asp Ile Ile Ser Phe Glu Gln Met Leu Lys Met Lys 325 330 335 Asp His Ala Leu Leu Gly Asn Ile Gly His Phe Asp Asn Glu Ile Asp 340 345 350 Met His Ser Leu Leu His Arg Asp Asp Val Thr Arg Thr Thr Ile Lys 355 360 365 Pro Gln Val Asp Glu Phe Thr Phe Ser Thr Gly Arg Ser Ile Ile Val 370 375 380 Leu Ser Glu Gly Arg Leu Leu Asn Leu Gly Asn Ala Thr Gly His Pro 385 390 395 400 Ser Phe Val Met Ser Asn Ser Phe Ala Asp Gln Thr Ile Ala Gln Ile 405 410 415 Glu Leu Phe Gln Asn Glu Gly Gln Tyr Glu Asn Glu Val Tyr Arg Leu 420 425 430 Pro Lys Val Leu Asp Glu Lys Val Ala Arg Ile His Val Glu Ala Leu 435 440 445 Gly Gly Gln Leu Thr Glu Leu Thr Lys Glu Gln Ala Glu Tyr Ile Gly 450 455 460 Val Asp Val Ala Gly Pro Phe Lys Pro Glu His Tyr Arg Tyr 465 470 475 99 128 DNA Corynebacterium glutamicum CDS (1)..(105) FRXA00132 99 cac gtt gag gct ctc ggc ggt cag ctc acc gaa ctg acc aag gag cag 48 His Val Glu Ala Leu Gly Gly Gln Leu Thr Glu Leu Thr Lys Glu Gln 1 5 10 15 gct gag tac atc ggc gtt gac gtt gca ggc cca ttc aag ccg gag cac 96 Ala Glu Tyr Ile Gly Val Asp Val Ala Gly Pro Phe Lys Pro Glu His 20 25 30 tac cgc tac taatgattgt cagcattgag gga 128 Tyr Arg Tyr 35 100 35 PRT Corynebacterium glutamicum 100 His Val Glu Ala Leu Gly Gly Gln Leu Thr Glu Leu Thr Lys Glu Gln 1 5 10 15 Ala Glu Tyr Ile Gly Val Asp Val Ala Gly Pro Phe Lys Pro Glu His 20 25 30 Tyr Arg Tyr 35 101 1396 DNA Corynebacterium glutamicum CDS (101)..(1396) FRXA01371 101 aacagcttca atcaattcgg tgtccactcc aacatgtaga gtggtgcgcg ttaaaaaagt 60 tttcctaatt ttcattttct taaaaggagc tcgccaggac atg gca cag gtt atg 115 Met Ala Gln Val Met 1 5 gac ttc aag gtt gcc gat ctt tca cta gca gag gca gga cgt cac cag 163 Asp Phe Lys Val Ala Asp Leu Ser Leu Ala Glu Ala Gly Arg His Gln 10 15 20 att cgt ctt gca gag tat gag atg cca ggt ctc atg cag ttg cgc aag 211 Ile Arg Leu Ala Glu Tyr Glu Met Pro Gly Leu Met Gln Leu Arg Lys 25 30 35 gaa ttc gca gac gag cag cct ttg aag ggc gcc cga att gct ggt tct 259 Glu Phe Ala Asp Glu Gln Pro Leu Lys Gly Ala Arg Ile Ala Gly Ser 40 45 50 atc cac atg acg gtc cag acc gcc gtg ctt att gag acc ctc act gct 307 Ile His Met Thr Val Gln Thr Ala Val Leu Ile Glu Thr Leu Thr Ala 55 60 65 ttg ggc gct gag gtt cgt tgg gct tcc tgc aac att ttc tcc acc cag 355 Leu Gly Ala Glu Val Arg Trp Ala Ser Cys Asn Ile Phe Ser Thr Gln 70 75 80 85 gat gag gct gca gcg gct atc gtt gtc ggc tcc ggc acc gtc gaa gag 403 Asp Glu Ala Ala Ala Ala Ile Val Val Gly Ser Gly Thr Val Glu Glu 90 95 100 cca gct ggt gtt cca gta ttc gcg tgg aag ggt gag tca ctg gag gag 451 Pro Ala Gly Val Pro Val Phe Ala Trp Lys Gly Glu Ser Leu Glu Glu 105 110 115 tac tgg tgg tgc atc aac cag atc ttc agc tgg ggc gat gag ctg cca 499 Tyr Trp Trp Cys Ile Asn Gln Ile Phe Ser Trp Gly Asp Glu Leu Pro 120 125 130 aac atg atc ctc gac gac ggc ggt gac gcc acc atg gct gtt att cgc 547 Asn Met Ile Leu Asp Asp Gly Gly Asp Ala Thr Met Ala Val Ile Arg 135 140 145 ggt cgc gaa tac gag cag gct ggt ctg gtt cca cca gca gag gcc aac 595 Gly Arg Glu Tyr Glu Gln Ala Gly Leu Val Pro Pro Ala Glu Ala Asn 150 155 160 165 gat tcc gat gag tac atc gca ttc ttg ggc atg ctg cgt gag gtt ctt 643 Asp Ser Asp Glu Tyr Ile Ala Phe Leu Gly Met Leu Arg Glu Val Leu 170 175 180 gct gca gag cct ggc aag tgg ggc aag atc gct gag gcc gtt aag ggt 691 Ala Ala Glu Pro Gly Lys Trp Gly Lys Ile Ala Glu Ala Val Lys Gly 185 190 195 gtc acc gag gaa acc acc acc ggt gtg cac cgc ctg tac cac ttc gct 739 Val Thr Glu Glu Thr Thr Thr Gly Val His Arg Leu Tyr His Phe Ala 200 205 210 gaa gaa ggc gtg ctg cct ttc cca gcg atg aac gtc aac gac gct gtc 787 Glu Glu Gly Val Leu Pro Phe Pro Ala Met Asn Val Asn Asp Ala Val 215 220 225 acc aag tcc aag ttt gat aac aag tac ggc acc cgc cac tcc ctg atc 835 Thr Lys Ser Lys Phe Asp Asn Lys Tyr Gly Thr Arg His Ser Leu Ile 230 235 240 245 gac ggc atc aac cgc gcc act gac atg ctc atg ggc ggc aag aac gtg 883 Asp Gly Ile Asn Arg Ala Thr Asp Met Leu Met Gly Gly Lys Asn Val 250 255 260 ctt gtc tgc ggt tac ggc gat gtc ggc aag ggc tgc gct gag gct ttc 931 Leu Val Cys Gly Tyr Gly Asp Val Gly Lys Gly Cys Ala Glu Ala Phe 265 270 275 gac ggc cag ggc gct cgc gtc aag gtc acc gaa gct gac cca atc aac 979 Asp Gly Gln Gly Ala Arg Val Lys Val Thr Glu Ala Asp Pro Ile Asn 280 285 290 gct ctt cag gct ctg atg gat ggc tac tct gtg gtc acc gtt gat gag 1027 Ala Leu Gln Ala Leu Met Asp Gly Tyr Ser Val Val Thr Val Asp Glu 295 300 305 gcc atc gag gac gcc gac atc gtg atc acc gcg acc ggc aac aag gac 1075 Ala Ile Glu Asp Ala Asp Ile Val Ile Thr Ala Thr Gly Asn Lys Asp 310 315 320 325 atc att tcc ttc gag cag atg ctc aag atg aag gat cac gct ctg ctg 1123 Ile Ile Ser Phe Glu Gln Met Leu Lys Met Lys Asp His Ala Leu Leu 330 335 340 ggc aac atc ggt cac ttt gat aat gag atc gat atg cat tcc ctg ttg 1171 Gly Asn Ile Gly His Phe Asp Asn Glu Ile Asp Met His Ser Leu Leu 345 350 355 cac cgc gac gac gtc acc cgc acc acg atc aag cca cag gtc gac gag 1219 His Arg Asp Asp Val Thr Arg Thr Thr Ile Lys Pro Gln Val Asp Glu 360 365 370 ttc acc ttc tcc acc ggt cgc tcc atc atc gtc ctg tcc gaa ggt cgc 1267 Phe Thr Phe Ser Thr Gly Arg Ser Ile Ile Val Leu Ser Glu Gly Arg 375 380 385 ctg ttg aac ctt ggc aac gcc acc gga cac cca tca ttt gtc atg tcc 1315 Leu Leu Asn Leu Gly Asn Ala Thr Gly His Pro Ser Phe Val Met Ser 390 395 400 405 aac tct ttc gcc gat cag acc att gcg cag atc gaa ctg ttc caa aac 1363 Asn Ser Phe Ala Asp Gln Thr Ile Ala Gln Ile Glu Leu Phe Gln Asn 410 415 420 gaa gga cag tac gag aac gag gtc tac cgt ctg 1396 Glu Gly Gln Tyr Glu Asn Glu Val Tyr Arg Leu 425 430 102 432 PRT Corynebacterium glutamicum 102 Met Ala Gln Val Met Asp Phe Lys Val Ala Asp Leu Ser Leu Ala Glu 1 5 10 15 Ala Gly Arg His Gln Ile Arg Leu Ala Glu Tyr Glu Met Pro Gly Leu 20 25 30 Met Gln Leu Arg Lys Glu Phe Ala Asp Glu Gln Pro Leu Lys Gly Ala 35 40 45 Arg Ile Ala Gly Ser Ile His Met Thr Val Gln Thr Ala Val Leu Ile 50 55 60 Glu Thr Leu Thr Ala Leu Gly Ala Glu Val Arg Trp Ala Ser Cys Asn 65 70 75 80 Ile Phe Ser Thr Gln Asp Glu Ala Ala Ala Ala Ile Val Val Gly Ser 85 90 95 Gly Thr Val Glu Glu Pro Ala Gly Val Pro Val Phe Ala Trp Lys Gly 100 105 110 Glu Ser Leu Glu Glu Tyr Trp Trp Cys Ile Asn Gln Ile Phe Ser Trp 115 120 125 Gly Asp Glu Leu Pro Asn Met Ile Leu Asp Asp Gly Gly Asp Ala Thr 130 135 140 Met Ala Val Ile Arg Gly Arg Glu Tyr Glu Gln Ala Gly Leu Val Pro 145 150 155 160 Pro Ala Glu Ala Asn Asp Ser Asp Glu Tyr Ile Ala Phe Leu Gly Met 165 170 175 Leu Arg Glu Val Leu Ala Ala Glu Pro Gly Lys Trp Gly Lys Ile Ala 180 185 190 Glu Ala Val Lys Gly Val Thr Glu Glu Thr Thr Thr Gly Val His Arg 195 200 205 Leu Tyr His Phe Ala Glu Glu Gly Val Leu Pro Phe Pro Ala Met Asn 210 215 220 Val Asn Asp Ala Val Thr Lys Ser Lys Phe Asp Asn Lys Tyr Gly Thr 225 230 235 240 Arg His Ser Leu Ile Asp Gly Ile Asn Arg Ala Thr Asp Met Leu Met 245 250 255 Gly Gly Lys Asn Val Leu Val Cys Gly Tyr Gly Asp Val Gly Lys Gly 260 265 270 Cys Ala Glu Ala Phe Asp Gly Gln Gly Ala Arg Val Lys Val Thr Glu 275 280 285 Ala Asp Pro Ile Asn Ala Leu Gln Ala Leu Met Asp Gly Tyr Ser Val 290 295 300 Val Thr Val Asp Glu Ala Ile Glu Asp Ala Asp Ile Val Ile Thr Ala 305 310 315 320 Thr Gly Asn Lys Asp Ile Ile Ser Phe Glu Gln Met Leu Lys Met Lys 325 330 335 Asp His Ala Leu Leu Gly Asn Ile Gly His Phe Asp Asn Glu Ile Asp 340 345 350 Met His Ser Leu Leu His Arg Asp Asp Val Thr Arg Thr Thr Ile Lys 355 360 365 Pro Gln Val Asp Glu Phe Thr Phe Ser Thr Gly Arg Ser Ile Ile Val 370 375 380 Leu Ser Glu Gly Arg Leu Leu Asn Leu Gly Asn Ala Thr Gly His Pro 385 390 395 400 Ser Phe Val Met Ser Asn Ser Phe Ala Asp Gln Thr Ile Ala Gln Ile 405 410 415 Glu Leu Phe Gln Asn Glu Gly Gln Tyr Glu Asn Glu Val Tyr Arg Leu 420 425 430 103 2358 DNA Corynebacterium glutamicum CDS (101)..(2335) RXN02085 103 cacccggtga tttcgcgaac cttgaaacat cgtcagaaga ttgccgtgcg tcctagccgg 60 gatccgcacg ttcggctcaa gcagaaagtc tttaactcac atg act tcc aac ttt 115 Met Thr Ser Asn Phe 1 5 tct tcc act gtc gct ggt ctt cct cgc atc gga gcg aag cgt gaa ctg 163 Ser Ser Thr Val Ala Gly Leu Pro Arg Ile Gly Ala Lys Arg Glu Leu 10 15 20 aag ttc gcg ctc gaa ggc tac tgg aat gga tca att gaa ggt cgc gaa 211 Lys Phe Ala Leu Glu Gly Tyr Trp Asn Gly Ser Ile Glu Gly Arg Glu 25 30 35 ctt gcg cag acc gcc cgc caa ttg gtc aac act gca tcg gat tct ttg 259 Leu Ala Gln Thr Ala Arg Gln Leu Val Asn Thr Ala Ser Asp Ser Leu 40 45 50 tct gga ttg gat tcc gtt ccg ttt gca gga cgt tcc tac tac gac gca 307 Ser Gly Leu Asp Ser Val Pro Phe Ala Gly Arg Ser Tyr Tyr Asp Ala 55 60 65 atg ctc gat acc gcc gct att ttg ggt gtg ctg ccg gag cgt ttt gat 355 Met Leu Asp Thr Ala Ala Ile Leu Gly Val Leu Pro Glu Arg Phe Asp 70 75 80 85 gac atc gct gat cat gaa aac gat ggt ctc cca ctg tgg att gac cgc 403 Asp Ile Ala Asp His Glu Asn Asp Gly Leu Pro Leu Trp Ile Asp Arg 90 95 100 tac ttt ggc gct gct cgc ggt act gag acc ctg cct gca cag gca atg 451 Tyr Phe Gly Ala Ala Arg Gly Thr Glu Thr Leu Pro Ala Gln Ala Met 105 110 115 acc aag tgg ttt gat acc aac tac cac tac ctc gtg ccg gag ttg tct 499 Thr Lys Trp Phe Asp Thr Asn Tyr His Tyr Leu Val Pro Glu Leu Ser 120 125 130 gcg gat aca cgt ttc gtt ttg gat gcg tcc gcg ctg att gag gat ctc 547 Ala Asp Thr Arg Phe Val Leu Asp Ala Ser Ala Leu Ile Glu Asp Leu 135 140 145 cgt tgc cag cag gtt cgt ggc gtt aat gcc cgc cct gtt ctg gtt ggt 595 Arg Cys Gln Gln Val Arg Gly Val Asn Ala Arg Pro Val Leu Val Gly 150 155 160 165 cca ctg act ttc ctt tcc ctt gct cgc acc act gat ggt tcc aat cct 643 Pro Leu Thr Phe Leu Ser Leu Ala Arg Thr Thr Asp Gly Ser Asn Pro 170 175 180 ttg gat cac ctg cct gca ctg ttt gag gtc tac gag cgc ctc atc aag 691 Leu Asp His Leu Pro Ala Leu Phe Glu Val Tyr Glu Arg Leu Ile Lys 185 190 195 tct ttc gat act gag tgg gtt cag atc gat gag cct gcg ttg gtc acc 739 Ser Phe Asp Thr Glu Trp Val Gln Ile Asp Glu Pro Ala Leu Val Thr 200 205 210 gat gtt gct cct gag gtt ttg gag cag gtc cgc gct ggt tac acc act 787 Asp Val Ala Pro Glu Val Leu Glu Gln Val Arg Ala Gly Tyr Thr Thr 215 220 225 ttg gct aag cgc gat ggc gtg ttt gtc aat act tac ttc ggc tct ggc 835 Leu Ala Lys Arg Asp Gly Val Phe Val Asn Thr Tyr Phe Gly Ser Gly 230 235 240 245 gat cag gcg ctg aac act ctt gcg ggc atc ggc ctt ggc gcg att ggc 883 Asp Gln Ala Leu Asn Thr Leu Ala Gly Ile Gly Leu Gly Ala Ile Gly 250 255 260 gtt gac ttg gtc acc cat ggc gtc act gag ctt gct gcg tgg aag ggt 931 Val Asp Leu Val Thr His Gly Val Thr Glu Leu Ala Ala Trp Lys Gly 265 270 275 gag gag ctg ctg gtt gcg ggc atc gtt gat ggt cgt aac att tgg cgc 979 Glu Glu Leu Leu Val Ala Gly Ile Val Asp Gly Arg Asn Ile Trp Arg 280 285 290 acc gac ctg tgt gct gct ctt gct tcc ctg aag cgc ctg gca gct cgc 1027 Thr Asp Leu Cys Ala Ala Leu Ala Ser Leu Lys Arg Leu Ala Ala Arg 295 300 305 ggc cca atc gca gtg tct acc tct tgt tca ctg ctg cac gtt cct tac 1075 Gly Pro Ile Ala Val Ser Thr Ser Cys Ser Leu Leu His Val Pro Tyr 310 315 320 325 acc ctc gag gct gag aac att gag cct gag gtc cgc gac tgg ctt gcc 1123 Thr Leu Glu Ala Glu Asn Ile Glu Pro Glu Val Arg Asp Trp Leu Ala 330 335 340 ttc ggc tcg gag aag atc acc gag gtc aag ctg ctt gcc gac gcc cta 1171 Phe Gly Ser Glu Lys Ile Thr Glu Val Lys Leu Leu Ala Asp Ala Leu 345 350 355 gcc ggc aac atc gac gcg gct gcg ttc gat gcg gcg tcc gca gca att 1219 Ala Gly Asn Ile Asp Ala Ala Ala Phe Asp Ala Ala Ser Ala Ala Ile 360 365 370 gct tct cga cgc acc tcc cca cgc acc gca cca atc acg cag gaa ctc 1267 Ala Ser Arg Arg Thr Ser Pro Arg Thr Ala Pro Ile Thr Gln Glu Leu 375 380 385 cct ggc cgt agc cgt gga tcc ttc gac act cgt gtt acg ctg cag gag 1315 Pro Gly Arg Ser Arg Gly Ser Phe Asp Thr Arg Val Thr Leu Gln Glu 390 395 400 405 aag tca ctg gag ctt cca gct ctg cca acc acc acc att ggt tct ttc 1363 Lys Ser Leu Glu Leu Pro Ala Leu Pro Thr Thr Thr Ile Gly Ser Phe 410 415 420 cca cag acc cca tcc att cgt tct gct cgc gct cgt ctg cgc aag gaa 1411 Pro Gln Thr Pro Ser Ile Arg Ser Ala Arg Ala Arg Leu Arg Lys Glu 425 430 435 tcc atc act ttg gag cag tac gaa gag gca atg cgc gaa gaa atc gat 1459 Ser Ile Thr Leu Glu Gln Tyr Glu Glu Ala Met Arg Glu Glu Ile Asp 440 445 450 ctg gtc atc gcc aag cag gaa gaa ctt ggt ctt gat gtg ttg gtt cac 1507 Leu Val Ile Ala Lys Gln Glu Glu Leu Gly Leu Asp Val Leu Val His 455 460 465 ggt gag cca gag cgc aac gac atg gtt cag tac ttc tct gaa ctt ctc 1555 Gly Glu Pro Glu Arg Asn Asp Met Val Gln Tyr Phe Ser Glu Leu Leu 470 475 480 485 gac ggt ttc ctc tca acc gcc aac ggc tgg gtc caa agc tac ggc tcc 1603 Asp Gly Phe Leu Ser Thr Ala Asn Gly Trp Val Gln Ser Tyr Gly Ser 490 495 500 cgc tgt gtt cgt cct cca gtg ttg ttc gga aac gtt tcc cgc cca gcg 1651 Arg Cys Val Arg Pro Pro Val Leu Phe Gly Asn Val Ser Arg Pro Ala 505 510 515 cca atg act gtc aag tgg ttc cag tac gca cag agc ctg acc cag aag 1699 Pro Met Thr Val Lys Trp Phe Gln Tyr Ala Gln Ser Leu Thr Gln Lys 520 525 530 cat gtc aag gga atg ctc acc ggt cca gtc acc atc ctt gca tgg tcc 1747 His Val Lys Gly Met Leu Thr Gly Pro Val Thr Ile Leu Ala Trp Ser 535 540 545 ttc gtt cgc gat gat cag ccg ctg gct acc act gct gac cag gtt gca 1795 Phe Val Arg Asp Asp Gln Pro Leu Ala Thr Thr Ala Asp Gln Val Ala 550 555 560 565 ctg gca ctg cgc gat gaa att aac gat ctc atc gag gct ggc gcg aag 1843 Leu Ala Leu Arg Asp Glu Ile Asn Asp Leu Ile Glu Ala Gly Ala Lys 570 575 580 atc atc cag gtg gat gag cct gcg att cgt gaa ctg ttg ccg cta cga 1891 Ile Ile Gln Val Asp Glu Pro Ala Ile Arg Glu Leu Leu Pro Leu Arg 585 590 595 gac gtc gat aag cct gcc tac ctg cag tgg tcc gtg gac tcc ttc cgc 1939 Asp Val Asp Lys Pro Ala Tyr Leu Gln Trp Ser Val Asp Ser Phe Arg 600 605 610 ctg gcg act gcc ggc gca ccc gac gac gtc caa atc cac acc cac atg 1987 Leu Ala Thr Ala Gly Ala Pro Asp Asp Val Gln Ile His Thr His Met 615 620 625 tgc tac tcc gag ttc aac gaa gtg atc tcc tcg gtc atc gcg ttg gat 2035 Cys Tyr Ser Glu Phe Asn Glu Val Ile Ser Ser Val Ile Ala Leu Asp 630 635 640 645 gcc gat gtc acc acc atc gaa gca gca cgt tcc gac atg cag gtc ctc 2083 Ala Asp Val Thr Thr Ile Glu Ala Ala Arg Ser Asp Met Gln Val Leu 650 655 660 gct gct ctg aaa tct tcc ggc ttc gag ctc ggc gtc gga cct ggt gtg 2131 Ala Ala Leu Lys Ser Ser Gly Phe Glu Leu Gly Val Gly Pro Gly Val 665 670 675 tgg gat atc cac tcc ccg cgc gtt cct tcc gcg cag aaa gtg gac ggt 2179 Trp Asp Ile His Ser Pro Arg Val Pro Ser Ala Gln Lys Val Asp Gly 680 685 690 ctc ctc gag gct gca ctg cag tcc gtg gat cct cgc cag ctg tgg gtc 2227 Leu Leu Glu Ala Ala Leu Gln Ser Val Asp Pro Arg Gln Leu Trp Val 695 700 705 aac cca gac tgt ggt ctg aag acc cgt gga tgg cca gaa gtg gaa gct 2275 Asn Pro Asp Cys Gly Leu Lys Thr Arg Gly Trp Pro Glu Val Glu Ala 710 715 720 725 tcc cta aag gtt ctc gtt gag tcc gct aag cag gct cgt gag aaa atc 2323 Ser Leu Lys Val Leu Val Glu Ser Ala Lys Gln Ala Arg Glu Lys Ile 730 735 740 gga gca act atc taaattgggt taccgctagg aac 2358 Gly Ala Thr Ile 745 104 745 PRT Corynebacterium glutamicum 104 Met Thr Ser Asn Phe Ser Ser Thr Val Ala Gly Leu Pro Arg Ile Gly 1 5 10 15 Ala Lys Arg Glu Leu Lys Phe Ala Leu Glu Gly Tyr Trp Asn Gly Ser 20 25 30 Ile Glu Gly Arg Glu Leu Ala Gln Thr Ala Arg Gln Leu Val Asn Thr 35 40 45 Ala Ser Asp Ser Leu Ser Gly Leu Asp Ser Val Pro Phe Ala Gly Arg 50 55 60 Ser Tyr Tyr Asp Ala Met Leu Asp Thr Ala Ala Ile Leu Gly Val Leu 65 70 75 80 Pro Glu Arg Phe Asp Asp Ile Ala Asp His Glu Asn Asp Gly Leu Pro 85 90 95 Leu Trp Ile Asp Arg Tyr Phe Gly Ala Ala Arg Gly Thr Glu Thr Leu 100 105 110 Pro Ala Gln Ala Met Thr Lys Trp Phe Asp Thr Asn Tyr His Tyr Leu 115 120 125 Val Pro Glu Leu Ser Ala Asp Thr Arg Phe Val Leu Asp Ala Ser Ala 130 135 140 Leu Ile Glu Asp Leu Arg Cys Gln Gln Val Arg Gly Val Asn Ala Arg 145 150 155 160 Pro Val Leu Val Gly Pro Leu Thr Phe Leu Ser Leu Ala Arg Thr Thr 165 170 175 Asp Gly Ser Asn Pro Leu Asp His Leu Pro Ala Leu Phe Glu Val Tyr 180 185 190 Glu Arg Leu Ile Lys Ser Phe Asp Thr Glu Trp Val Gln Ile Asp Glu 195 200 205 Pro Ala Leu Val Thr Asp Val Ala Pro Glu Val Leu Glu Gln Val Arg 210 215 220 Ala Gly Tyr Thr Thr Leu Ala Lys Arg Asp Gly Val Phe Val Asn Thr 225 230 235 240 Tyr Phe Gly Ser Gly Asp Gln Ala Leu Asn Thr Leu Ala Gly Ile Gly 245 250 255 Leu Gly Ala Ile Gly Val Asp Leu Val Thr His Gly Val Thr Glu Leu 260 265 270 Ala Ala Trp Lys Gly Glu Glu Leu Leu Val Ala Gly Ile Val Asp Gly 275 280 285 Arg Asn Ile Trp Arg Thr Asp Leu Cys Ala Ala Leu Ala Ser Leu Lys 290 295 300 Arg Leu Ala Ala Arg Gly Pro Ile Ala Val Ser Thr Ser Cys Ser Leu 305 310 315 320 Leu His Val Pro Tyr Thr Leu Glu Ala Glu Asn Ile Glu Pro Glu Val 325 330 335 Arg Asp Trp Leu Ala Phe Gly Ser Glu Lys Ile Thr Glu Val Lys Leu 340 345 350 Leu Ala Asp Ala Leu Ala Gly Asn Ile Asp Ala Ala Ala Phe Asp Ala 355 360 365 Ala Ser Ala Ala Ile Ala Ser Arg Arg Thr Ser Pro Arg Thr Ala Pro 370 375 380 Ile Thr Gln Glu Leu Pro Gly Arg Ser Arg Gly Ser Phe Asp Thr Arg 385 390 395 400 Val Thr Leu Gln Glu Lys Ser Leu Glu Leu Pro Ala Leu Pro Thr Thr 405 410 415 Thr Ile Gly Ser Phe Pro Gln Thr Pro Ser Ile Arg Ser Ala Arg Ala 420 425 430 Arg Leu Arg Lys Glu Ser Ile Thr Leu Glu Gln Tyr Glu Glu Ala Met 435 440 445 Arg Glu Glu Ile Asp Leu Val Ile Ala Lys Gln Glu Glu Leu Gly Leu 450 455 460 Asp Val Leu Val His Gly Glu Pro Glu Arg Asn Asp Met Val Gln Tyr 465 470 475 480 Phe Ser Glu Leu Leu Asp Gly Phe Leu Ser Thr Ala Asn Gly Trp Val 485 490 495 Gln Ser Tyr Gly Ser Arg Cys Val Arg Pro Pro Val Leu Phe Gly Asn 500 505 510 Val Ser Arg Pro Ala Pro Met Thr Val Lys Trp Phe Gln Tyr Ala Gln 515 520 525 Ser Leu Thr Gln Lys His Val Lys Gly Met Leu Thr Gly Pro Val Thr 530 535 540 Ile Leu Ala Trp Ser Phe Val Arg Asp Asp Gln Pro Leu Ala Thr Thr 545 550 555 560 Ala Asp Gln Val Ala Leu Ala Leu Arg Asp Glu Ile Asn Asp Leu Ile 565 570 575 Glu Ala Gly Ala Lys Ile Ile Gln Val Asp Glu Pro Ala Ile Arg Glu 580 585 590 Leu Leu Pro Leu Arg Asp Val Asp Lys Pro Ala Tyr Leu Gln Trp Ser 595 600 605 Val Asp Ser Phe Arg Leu Ala Thr Ala Gly Ala Pro Asp Asp Val Gln 610 615 620 Ile His Thr His Met Cys Tyr Ser Glu Phe Asn Glu Val Ile Ser Ser 625 630 635 640 Val Ile Ala Leu Asp Ala Asp Val Thr Thr Ile Glu Ala Ala Arg Ser 645 650 655 Asp Met Gln Val Leu Ala Ala Leu Lys Ser Ser Gly Phe Glu Leu Gly 660 665 670 Val Gly Pro Gly Val Trp Asp Ile His Ser Pro Arg Val Pro Ser Ala 675 680 685 Gln Lys Val Asp Gly Leu Leu Glu Ala Ala Leu Gln Ser Val Asp Pro 690 695 700 Arg Gln Leu Trp Val Asn Pro Asp Cys Gly Leu Lys Thr Arg Gly Trp 705 710 715 720 Pro Glu Val Glu Ala Ser Leu Lys Val Leu Val Glu Ser Ala Lys Gln 725 730 735 Ala Arg Glu Lys Ile Gly Ala Thr Ile 740 745 105 1923 DNA Corynebacterium glutamicum CDS (101)..(1900) FRXA02085 105 cacccggtga tttcgcgaac cttgaaacat cgtcagaaga ttgccgtgcg tcctagccgg 60 gatccgcacg ttcggctcaa gcagaaagtc tttaactcac atg act tcc aac ttt 115 Met Thr Ser Asn Phe 1 5 tct tcc act gtc gct ggt ctt cct cgc atc gga gcg aag cgt gaa ctg 163 Ser Ser Thr Val Ala Gly Leu Pro Arg Ile Gly Ala Lys Arg Glu Leu 10 15 20 aag ttc gcg ctc gaa ggc tac tgg aat gga tca att gaa ggt cgc gaa 211 Lys Phe Ala Leu Glu Gly Tyr Trp Asn Gly Ser Ile Glu Gly Arg Glu 25 30 35 ctt gcg cag acc gcc cgc caa ttg gtc aac act gca tcg gat tct ttg 259 Leu Ala Gln Thr Ala Arg Gln Leu Val Asn Thr Ala Ser Asp Ser Leu 40 45 50 tct gga ttg gat tcc gtt ccg ttt gca gga cgt tcc tac tac gac gca 307 Ser Gly Leu Asp Ser Val Pro Phe Ala Gly Arg Ser Tyr Tyr Asp Ala 55 60 65 atg ctc gat acc gcc gct att ttg ggt gtg ctg ccg gag cgt ttt gat 355 Met Leu Asp Thr Ala Ala Ile Leu Gly Val Leu Pro Glu Arg Phe Asp 70 75 80 85 gac atc gct gat cat gaa aac gat ggt ctc cca ctg tgg att gac cgc 403 Asp Ile Ala Asp His Glu Asn Asp Gly Leu Pro Leu Trp Ile Asp Arg 90 95 100 tac ttt ggc gct gct cgc ggt act gag acc ctg cct gca cag gca atg 451 Tyr Phe Gly Ala Ala Arg Gly Thr Glu Thr Leu Pro Ala Gln Ala Met 105 110 115 acc aag tgg ttt gat acc aac tac cac tac ctc gtg ccg gag ttg tct 499 Thr Lys Trp Phe Asp Thr Asn Tyr His Tyr Leu Val Pro Glu Leu Ser 120 125 130 gcg gat aca cgt ttc gtt ttg gat gcg tcc gcg ctg att gag gat ctc 547 Ala Asp Thr Arg Phe Val Leu Asp Ala Ser Ala Leu Ile Glu Asp Leu 135 140 145 cgt tgc cag cag gtt cgt ggc gtt aat gcc cgc cct gtt ctg gtt ggt 595 Arg Cys Gln Gln Val Arg Gly Val Asn Ala Arg Pro Val Leu Val Gly 150 155 160 165 cca ctg act ttc ctt tcc ctt gct cgc acc act gat ggt tcc aat cct 643 Pro Leu Thr Phe Leu Ser Leu Ala Arg Thr Thr Asp Gly Ser Asn Pro 170 175 180 ttg gat cac ctg cct gca ctg ttt gag gtc tac gag cgc ctc atc aag 691 Leu Asp His Leu Pro Ala Leu Phe Glu Val Tyr Glu Arg Leu Ile Lys 185 190 195 tct ttc gat act gag tgg gtt cag atc gat gag cct gcg ttg gtc acc 739 Ser Phe Asp Thr Glu Trp Val Gln Ile Asp Glu Pro Ala Leu Val Thr 200 205 210 gat gtt gct cct gag gtt ttg gag cag gtc cgc gct ggt tac acc act 787 Asp Val Ala Pro Glu Val Leu Glu Gln Val Arg Ala Gly Tyr Thr Thr 215 220 225 ttg gct aag cgc gat ggc gtg ttt gtc aat act tac ttc ggc tct ggc 835 Leu Ala Lys Arg Asp Gly Val Phe Val Asn Thr Tyr Phe Gly Ser Gly 230 235 240 245 gat cag gcg ctg aac act ctt gcg ggc atc ggc ctt ggc gcg att ggc 883 Asp Gln Ala Leu Asn Thr Leu Ala Gly Ile Gly Leu Gly Ala Ile Gly 250 255 260 gtt gac ttg gtc acc cat ggc gtc act gag ctt gct gcg tgg aag ggt 931 Val Asp Leu Val Thr His Gly Val Thr Glu Leu Ala Ala Trp Lys Gly 265 270 275 gag gag ctg ctg gtt gcg ggc atc gtt gat ggt cgt aac att tgg cgc 979 Glu Glu Leu Leu Val Ala Gly Ile Val Asp Gly Arg Asn Ile Trp Arg 280 285 290 acc gac ctg tgt gct gct ctt gct tcc ctg aag cgc ctg gca gct cgc 1027 Thr Asp Leu Cys Ala Ala Leu Ala Ser Leu Lys Arg Leu Ala Ala Arg 295 300 305 ggc cca atc gca gtg tct acc tct tgt tca ctg ctg cac gtt cct tac 1075 Gly Pro Ile Ala Val Ser Thr Ser Cys Ser Leu Leu His Val Pro Tyr 310 315 320 325 acc ctc gag gct gag aac att gag cct gag gtc cgc gac tgg ctt gcc 1123 Thr Leu Glu Ala Glu Asn Ile Glu Pro Glu Val Arg Asp Trp Leu Ala 330 335 340 ttc ggc tcg gag aag atc acc gag gtc aag ctg ctt gcc gac gcc cta 1171 Phe Gly Ser Glu Lys Ile Thr Glu Val Lys Leu Leu Ala Asp Ala Leu 345 350 355 gcc ggc aac atc gac gcg gct gcg ttc gat gcg gcg tcc gca gca att 1219 Ala Gly Asn Ile Asp Ala Ala Ala Phe Asp Ala Ala Ser Ala Ala Ile 360 365 370 gct tct cga cgc acc tcc cca cgc acc gca cca atc acg cag gaa ctc 1267 Ala Ser Arg Arg Thr Ser Pro Arg Thr Ala Pro Ile Thr Gln Glu Leu 375 380 385 cct ggc cgt agc cgt gga tcc ttc gac act cgt gtt acg ctg cag gag 1315 Pro Gly Arg Ser Arg Gly Ser Phe Asp Thr Arg Val Thr Leu Gln Glu 390 395 400 405 aag tca ctg gag ctt cca gct ctg cca acc acc acc att ggt tct ttc 1363 Lys Ser Leu Glu Leu Pro Ala Leu Pro Thr Thr Thr Ile Gly Ser Phe 410 415 420 cca cag acc cca tcc att cgt tct gct cgc gct cgt ctg cgc aag gaa 1411 Pro Gln Thr Pro Ser Ile Arg Ser Ala Arg Ala Arg Leu Arg Lys Glu 425 430 435 tcc atc act ttg gag cag tac gaa gag gca atg cgc gaa gaa atc gat 1459 Ser Ile Thr Leu Glu Gln Tyr Glu Glu Ala Met Arg Glu Glu Ile Asp 440 445 450 ctg gtc atc gcc aag cag gaa gaa ctt ggt ctt gat gtg ttg gtt cac 1507 Leu Val Ile Ala Lys Gln Glu Glu Leu Gly Leu Asp Val Leu Val His 455 460 465 ggt gag cca gag cgc aac gac atg gtt cag tac ttc tct gaa ctt ctc 1555 Gly Glu Pro Glu Arg Asn Asp Met Val Gln Tyr Phe Ser Glu Leu Leu 470 475 480 485 gac ggt ttc ctc tca acc gcc aac ggc tgg gtc caa agc tac ggc tcc 1603 Asp Gly Phe Leu Ser Thr Ala Asn Gly Trp Val Gln Ser Tyr Gly Ser 490 495 500 cgc tgt gtt cgt cct cca gtg ttg ttc gga aac gtt tcc cgc cca gcg 1651 Arg Cys Val Arg Pro Pro Val Leu Phe Gly Asn Val Ser Arg Pro Ala 505 510 515 cca atg act gtc aag tgg ttc cag tac gca cag agc ctg acc cag aag 1699 Pro Met Thr Val Lys Trp Phe Gln Tyr Ala Gln Ser Leu Thr Gln Lys 520 525 530 cat gtc aag gga atg ctc acc ggt cca gtc acc atc ctt gca tgg tcc 1747 His Val Lys Gly Met Leu Thr Gly Pro Val Thr Ile Leu Ala Trp Ser 535 540 545 ttc gtt cgc gat gat cag ccg ctg gct acc act gct gac cag gtt gca 1795 Phe Val Arg Asp Asp Gln Pro Leu Ala Thr Thr Ala Asp Gln Val Ala 550 555 560 565 ctg gca ctg cgc gat gaa att aac gat ctc atc gag gct ggc gcg aag 1843 Leu Ala Leu Arg Asp Glu Ile Asn Asp Leu Ile Glu Ala Gly Ala Lys 570 575 580 atc atc cag gtg gat gag cct gcg att cgt gaa ctg ttg ccc gct acg 1891 Ile Ile Gln Val Asp Glu Pro Ala Ile Arg Glu Leu Leu Pro Ala Thr 585 590 595 aga cgt cga taagcctgcc tacctgcagt ggt 1923 Arg Arg Arg 600 106 600 PRT Corynebacterium glutamicum 106 Met Thr Ser Asn Phe Ser Ser Thr Val Ala Gly Leu Pro Arg Ile Gly 1 5 10 15 Ala Lys Arg Glu Leu Lys Phe Ala Leu Glu Gly Tyr Trp Asn Gly Ser 20 25 30 Ile Glu Gly Arg Glu Leu Ala Gln Thr Ala Arg Gln Leu Val Asn Thr 35 40 45 Ala Ser Asp Ser Leu Ser Gly Leu Asp Ser Val Pro Phe Ala Gly Arg 50 55 60 Ser Tyr Tyr Asp Ala Met Leu Asp Thr Ala Ala Ile Leu Gly Val Leu 65 70 75 80 Pro Glu Arg Phe Asp Asp Ile Ala Asp His Glu Asn Asp Gly Leu Pro 85 90 95 Leu Trp Ile Asp Arg Tyr Phe Gly Ala Ala Arg Gly Thr Glu Thr Leu 100 105 110 Pro Ala Gln Ala Met Thr Lys Trp Phe Asp Thr Asn Tyr His Tyr Leu 115 120 125 Val Pro Glu Leu Ser Ala Asp Thr Arg Phe Val Leu Asp Ala Ser Ala 130 135 140 Leu Ile Glu Asp Leu Arg Cys Gln Gln Val Arg Gly Val Asn Ala Arg 145 150 155 160 Pro Val Leu Val Gly Pro Leu Thr Phe Leu Ser Leu Ala Arg Thr Thr 165 170 175 Asp Gly Ser Asn Pro Leu Asp His Leu Pro Ala Leu Phe Glu Val Tyr 180 185 190 Glu Arg Leu Ile Lys Ser Phe Asp Thr Glu Trp Val Gln Ile Asp Glu 195 200 205 Pro Ala Leu Val Thr Asp Val Ala Pro Glu Val Leu Glu Gln Val Arg 210 215 220 Ala Gly Tyr Thr Thr Leu Ala Lys Arg Asp Gly Val Phe Val Asn Thr 225 230 235 240 Tyr Phe Gly Ser Gly Asp Gln Ala Leu Asn Thr Leu Ala Gly Ile Gly 245 250 255 Leu Gly Ala Ile Gly Val Asp Leu Val Thr His Gly Val Thr Glu Leu 260 265 270 Ala Ala Trp Lys Gly Glu Glu Leu Leu Val Ala Gly Ile Val Asp Gly 275 280 285 Arg Asn Ile Trp Arg Thr Asp Leu Cys Ala Ala Leu Ala Ser Leu Lys 290 295 300 Arg Leu Ala Ala Arg Gly Pro Ile Ala Val Ser Thr Ser Cys Ser Leu 305 310 315 320 Leu His Val Pro Tyr Thr Leu Glu Ala Glu Asn Ile Glu Pro Glu Val 325 330 335 Arg Asp Trp Leu Ala Phe Gly Ser Glu Lys Ile Thr Glu Val Lys Leu 340 345 350 Leu Ala Asp Ala Leu Ala Gly Asn Ile Asp Ala Ala Ala Phe Asp Ala 355 360 365 Ala Ser Ala Ala Ile Ala Ser Arg Arg Thr Ser Pro Arg Thr Ala Pro 370 375 380 Ile Thr Gln Glu Leu Pro Gly Arg Ser Arg Gly Ser Phe Asp Thr Arg 385 390 395 400 Val Thr Leu Gln Glu Lys Ser Leu Glu Leu Pro Ala Leu Pro Thr Thr 405 410 415 Thr Ile Gly Ser Phe Pro Gln Thr Pro Ser Ile Arg Ser Ala Arg Ala 420 425 430 Arg Leu Arg Lys Glu Ser Ile Thr Leu Glu Gln Tyr Glu Glu Ala Met 435 440 445 Arg Glu Glu Ile Asp Leu Val Ile Ala Lys Gln Glu Glu Leu Gly Leu 450 455 460 Asp Val Leu Val His Gly Glu Pro Glu Arg Asn Asp Met Val Gln Tyr 465 470 475 480 Phe Ser Glu Leu Leu Asp Gly Phe Leu Ser Thr Ala Asn Gly Trp Val 485 490 495 Gln Ser Tyr Gly Ser Arg Cys Val Arg Pro Pro Val Leu Phe Gly Asn 500 505 510 Val Ser Arg Pro Ala Pro Met Thr Val Lys Trp Phe Gln Tyr Ala Gln 515 520 525 Ser Leu Thr Gln Lys His Val Lys Gly Met Leu Thr Gly Pro Val Thr 530 535 540 Ile Leu Ala Trp Ser Phe Val Arg Asp Asp Gln Pro Leu Ala Thr Thr 545 550 555 560 Ala Asp Gln Val Ala Leu Ala Leu Arg Asp Glu Ile Asn Asp Leu Ile 565 570 575 Glu Ala Gly Ala Lys Ile Ile Gln Val Asp Glu Pro Ala Ile Arg Glu 580 585 590 Leu Leu Pro Ala Thr Arg Arg Arg 595 600 107 603 DNA Corynebacterium glutamicum CDS (101)..(580) FRXA02086 107 gatgatcagc cgctggctac cactgctgac caggttgcac tggcactgcg cgatgaaatt 60 aacgatctca tcgaggctgg cgcgaagatc atccaggtgg atg agc ctg cga ttc 115 Met Ser Leu Arg Phe 1 5 gtg aac tgt tgc ccg cta cga gac gtc gat aag cct gcc tac ctg cag 163 Val Asn Cys Cys Pro Leu Arg Asp Val Asp Lys Pro Ala Tyr Leu Gln 10 15 20 tgg tcc gtg gac tcc ttc cgc ctg gcg act gcc ggc gca ccc gac gac 211 Trp Ser Val Asp Ser Phe Arg Leu Ala Thr Ala Gly Ala Pro Asp Asp 25 30 35 gtc caa atc cac acc cac atg tgc tac tcc gag ttc aac gaa gtg atc 259 Val Gln Ile His Thr His Met Cys Tyr Ser Glu Phe Asn Glu Val Ile 40 45 50 tcc tcg gtc atc gcg ttg gat gcc gat gtc acc acc atc gaa gca gca 307 Ser Ser Val Ile Ala Leu Asp Ala Asp Val Thr Thr Ile Glu Ala Ala 55 60 65 cgt tcc gac atg cag gtc ctc gct gct ctg aaa tct tcc ggc ttc gag 355 Arg Ser Asp Met Gln Val Leu Ala Ala Leu Lys Ser Ser Gly Phe Glu 70 75 80 85 ctc ggc gtc gga cct ggt gtg tgg gat atc cac tcc ccg cgc gtt cct 403 Leu Gly Val Gly Pro Gly Val Trp Asp Ile His Ser Pro Arg Val Pro 90 95 100 tcc gcg cag aaa gtg gac ggt ctc ctc gag gct gca ctg cag tcc gtg 451 Ser Ala Gln Lys Val Asp Gly Leu Leu Glu Ala Ala Leu Gln Ser Val 105 110 115 gat cct cgc cag ctg tgg gtc aac cca gac tgt ggt ctg aag acc cgt 499 Asp Pro Arg Gln Leu Trp Val Asn Pro Asp Cys Gly Leu Lys Thr Arg 120 125 130 gga tgg cca gaa gtg gaa gct tcc cta aag gtt ctc gtt gag tcc gct 547 Gly Trp Pro Glu Val Glu Ala Ser Leu Lys Val Leu Val Glu Ser Ala 135 140 145 aag cag gct cgt gag aaa atc gga gca act atc taaattgggt taccgctagg 600 Lys Gln Ala Arg Glu Lys Ile Gly Ala Thr Ile 150 155 160 aac 603 108 160 PRT Corynebacterium glutamicum 108 Met Ser Leu Arg Phe Val Asn Cys Cys Pro Leu Arg Asp Val Asp Lys 1 5 10 15 Pro Ala Tyr Leu Gln Trp Ser Val Asp Ser Phe Arg Leu Ala Thr Ala 20 25 30 Gly Ala Pro Asp Asp Val Gln Ile His Thr His Met Cys Tyr Ser Glu 35 40 45 Phe Asn Glu Val Ile Ser Ser Val Ile Ala Leu Asp Ala Asp Val Thr 50 55 60 Thr Ile Glu Ala Ala Arg Ser Asp Met Gln Val Leu Ala Ala Leu Lys 65 70 75 80 Ser Ser Gly Phe Glu Leu Gly Val Gly Pro Gly Val Trp Asp Ile His 85 90 95 Ser Pro Arg Val Pro Ser Ala Gln Lys Val Asp Gly Leu Leu Glu Ala 100 105 110 Ala Leu Gln Ser Val Asp Pro Arg Gln Leu Trp Val Asn Pro Asp Cys 115 120 125 Gly Leu Lys Thr Arg Gly Trp Pro Glu Val Glu Ala Ser Leu Lys Val 130 135 140 Leu Val Glu Ser Ala Lys Gln Ala Arg Glu Lys Ile Gly Ala Thr Ile 145 150 155 160 109 1326 DNA Corynebacterium glutamicum CDS (101)..(1303) RXN02648 109 atgaataaaa ttccgggtgc agtgaccgta ggtgaggtaa acgcggttag agtcgaatga 60 gagtttgata ctttctttcg acttttagat tggattttca atg agc cag aac cgc 115 Met Ser Gln Asn Arg 1 5 atc agg acc act cac gtt ggt tcc ttg ccc cgt acc cca gag cta ctt 163 Ile Arg Thr Thr His Val Gly Ser Leu Pro Arg Thr Pro Glu Leu Leu 10 15 20 gat gca aac atc aag cgt tct aac ggt gag att ggg gag gag gaa ttc 211 Asp Ala Asn Ile Lys Arg Ser Asn Gly Glu Ile Gly Glu Glu Glu Phe 25 30 35 ttc cag att ctg cag tct tct gta gat gac gtg atc aag cgc cag gtt 259 Phe Gln Ile Leu Gln Ser Ser Val Asp Asp Val Ile Lys Arg Gln Val 40 45 50 gac ctg ggt atc gac atc ctt aac gag ggc gaa tac ggc cac gtc acc 307 Asp Leu Gly Ile Asp Ile Leu Asn Glu Gly Glu Tyr Gly His Val Thr 55 60 65 tcc ggt gca gtt gac ttc ggt gca tgg tgg aac tac tcc ttc acc cgc 355 Ser Gly Ala Val Asp Phe Gly Ala Trp Trp Asn Tyr Ser Phe Thr Arg 70 75 80 85 ctg ggc gga ctg acc atg acc gat acc gac cgt tgg gca agc cag gaa 403 Leu Gly Gly Leu Thr Met Thr Asp Thr Asp Arg Trp Ala Ser Gln Glu 90 95 100 gca gtg cgt tcc acc cct ggc aac atc gag ctg acc agc ttc tct gat 451 Ala Val Arg Ser Thr Pro Gly Asn Ile Glu Leu Thr Ser Phe Ser Asp 105 110 115 cgt cgc gac cgc gca ttg ttc agc gaa gca tac gag gat cca gta tct 499 Arg Arg Asp Arg Ala Leu Phe Ser Glu Ala Tyr Glu Asp Pro Val Ser 120 125 130 ggc atc ttc acc ggt cgc gct tct gtg ggc aac cca gag ttc acc gga 547 Gly Ile Phe Thr Gly Arg Ala Ser Val Gly Asn Pro Glu Phe Thr Gly 135 140 145 cct att acc tac att ggc cag gaa gaa act cag acg gat gtt gat ctg 595 Pro Ile Thr Tyr Ile Gly Gln Glu Glu Thr Gln Thr Asp Val Asp Leu 150 155 160 165 ctg aag aag ggc atg aac gca gcg gga gct acc gac ggc ttc gtt gca 643 Leu Lys Lys Gly Met Asn Ala Ala Gly Ala Thr Asp Gly Phe Val Ala 170 175 180 gca cta tcc cca gga tct gca gct cga ttg acc aac aag ttc tac gac 691 Ala Leu Ser Pro Gly Ser Ala Ala Arg Leu Thr Asn Lys Phe Tyr Asp 185 190 195 act gat gaa gaa gtc gtc gca gca tgt gct gat gcg ctt tcc cag gaa 739 Thr Asp Glu Glu Val Val Ala Ala Cys Ala Asp Ala Leu Ser Gln Glu 200 205 210 tac aag atc atc acc gat gca ggt ctg acc gtt cag ctc gac gca ccg 787 Tyr Lys Ile Ile Thr Asp Ala Gly Leu Thr Val Gln Leu Asp Ala Pro 215 220 225 gac ttg gca gaa gca tgg gat cag atc aac cca gag cca agc gtg aag 835 Asp Leu Ala Glu Ala Trp Asp Gln Ile Asn Pro Glu Pro Ser Val Lys 230 235 240 245 gat tac ttg gac tgg atc ggt aca cgc atc gat gcc atc aac agt gca 883 Asp Tyr Leu Asp Trp Ile Gly Thr Arg Ile Asp Ala Ile Asn Ser Ala 250 255 260 gtg aag ggc ctt cca aag gaa cag acc cgc ctg cac atc tgc tgg ggc 931 Val Lys Gly Leu Pro Lys Glu Gln Thr Arg Leu His Ile Cys Trp Gly 265 270 275 tct tgg cac gga cca cac gtc act gac atc cca ttc ggt gac atc att 979 Ser Trp His Gly Pro His Val Thr Asp Ile Pro Phe Gly Asp Ile Ile 280 285 290 ggt gag atc ctg cgc gca gag gtc ggt ggc ttc tcc ttc gaa ggc gca 1027 Gly Glu Ile Leu Arg Ala Glu Val Gly Gly Phe Ser Phe Glu Gly Ala 295 300 305 tct cct cgt cac gca cac gag tgg cgt gta tgg gaa gaa aac aag ctt 1075 Ser Pro Arg His Ala His Glu Trp Arg Val Trp Glu Glu Asn Lys Leu 310 315 320 325 cct gaa ggc tct gtt atc tac cct ggt gtt gtg tct cac tcc atc aac 1123 Pro Glu Gly Ser Val Ile Tyr Pro Gly Val Val Ser His Ser Ile Asn 330 335 340 gct gtg gag cac cca cgc ctg gtt gct gat cgt atc gtt cag ttc gcc 1171 Ala Val Glu His Pro Arg Leu Val Ala Asp Arg Ile Val Gln Phe Ala 345 350 355 aag ctt gtt ggc cct gag aac gtc att gcg tcc act gac tgt ggt ctg 1219 Lys Leu Val Gly Pro Glu Asn Val Ile Ala Ser Thr Asp Cys Gly Leu 360 365 370 ggc gga cgt ctg cat tcc cag atc gca tgg gca aag ctg gag tcc cta 1267 Gly Gly Arg Leu His Ser Gln Ile Ala Trp Ala Lys Leu Glu Ser Leu 375 380 385 gta gag ggc gct cgc att gca tca aag gaa ctg ttc taagctagac 1313 Val Glu Gly Ala Arg Ile Ala Ser Lys Glu Leu Phe 390 395 400 aacgagggtt gct 1326 110 401 PRT Corynebacterium glutamicum 110 Met Ser Gln Asn Arg Ile Arg Thr Thr His Val Gly Ser Leu Pro Arg 1 5 10 15 Thr Pro Glu Leu Leu Asp Ala Asn Ile Lys Arg Ser Asn Gly Glu Ile 20 25 30 Gly Glu Glu Glu Phe Phe Gln Ile Leu Gln Ser Ser Val Asp Asp Val 35 40 45 Ile Lys Arg Gln Val Asp Leu Gly Ile Asp Ile Leu Asn Glu Gly Glu 50 55 60 Tyr Gly His Val Thr Ser Gly Ala Val Asp Phe Gly Ala Trp Trp Asn 65 70 75 80 Tyr Ser Phe Thr Arg Leu Gly Gly Leu Thr Met Thr Asp Thr Asp Arg 85 90 95 Trp Ala Ser Gln Glu Ala Val Arg Ser Thr Pro Gly Asn Ile Glu Leu 100 105 110 Thr Ser Phe Ser Asp Arg Arg Asp Arg Ala Leu Phe Ser Glu Ala Tyr 115 120 125 Glu Asp Pro Val Ser Gly Ile Phe Thr Gly Arg Ala Ser Val Gly Asn 130 135 140 Pro Glu Phe Thr Gly Pro Ile Thr Tyr Ile Gly Gln Glu Glu Thr Gln 145 150 155 160 Thr Asp Val Asp Leu Leu Lys Lys Gly Met Asn Ala Ala Gly Ala Thr 165 170 175 Asp Gly Phe Val Ala Ala Leu Ser Pro Gly Ser Ala Ala Arg Leu Thr 180 185 190 Asn Lys Phe Tyr Asp Thr Asp Glu Glu Val Val Ala Ala Cys Ala Asp 195 200 205 Ala Leu Ser Gln Glu Tyr Lys Ile Ile Thr Asp Ala Gly Leu Thr Val 210 215 220 Gln Leu Asp Ala Pro Asp Leu Ala Glu Ala Trp Asp Gln Ile Asn Pro 225 230 235 240 Glu Pro Ser Val Lys Asp Tyr Leu Asp Trp Ile Gly Thr Arg Ile Asp 245 250 255 Ala Ile Asn Ser Ala Val Lys Gly Leu Pro Lys Glu Gln Thr Arg Leu 260 265 270 His Ile Cys Trp Gly Ser Trp His Gly Pro His Val Thr Asp Ile Pro 275 280 285 Phe Gly Asp Ile Ile Gly Glu Ile Leu Arg Ala Glu Val Gly Gly Phe 290 295 300 Ser Phe Glu Gly Ala Ser Pro Arg His Ala His Glu Trp Arg Val Trp 305 310 315 320 Glu Glu Asn Lys Leu Pro Glu Gly Ser Val Ile Tyr Pro Gly Val Val 325 330 335 Ser His Ser Ile Asn Ala Val Glu His Pro Arg Leu Val Ala Asp Arg 340 345 350 Ile Val Gln Phe Ala Lys Leu Val Gly Pro Glu Asn Val Ile Ala Ser 355 360 365 Thr Asp Cys Gly Leu Gly Gly Arg Leu His Ser Gln Ile Ala Trp Ala 370 375 380 Lys Leu Glu Ser Leu Val Glu Gly Ala Arg Ile Ala Ser Lys Glu Leu 385 390 395 400 Phe 111 548 DNA Corynebacterium glutamicum CDS (1)..(525) FRXA02648 111 gac gca ccg gac ttg gca gaa gca tgg gat cag atc aac cca gag cca 48 Asp Ala Pro Asp Leu Ala Glu Ala Trp Asp Gln Ile Asn Pro Glu Pro 1 5 10 15 agc gtg aag gat tac ttg gac tgg atc ggt aca cgc atc gat gcc atc 96 Ser Val Lys Asp Tyr Leu Asp Trp Ile Gly Thr Arg Ile Asp Ala Ile 20 25 30 aac agt gca gtg aag ggc ctt cca aag gaa cag acc cgc ctg cac atc 144 Asn Ser Ala Val Lys Gly Leu Pro Lys Glu Gln Thr Arg Leu His Ile 35 40 45 tgc tgg ggc tct tgg cac gga cca cac gtc act gac atc cca ttc ggt 192 Cys Trp Gly Ser Trp His Gly Pro His Val Thr Asp Ile Pro Phe Gly 50 55 60 gac atc att ggt gag atc ctg cgc gca gag gtc ggt ggc ttc tcc ttc 240 Asp Ile Ile Gly Glu Ile Leu Arg Ala Glu Val Gly Gly Phe Ser Phe 65 70 75 80 gaa ggc gca tct cct cgt cac gca cac gag tgg cgt gta tgg gaa gaa 288 Glu Gly Ala Ser Pro Arg His Ala His Glu Trp Arg Val Trp Glu Glu 85 90 95 aac aag ctt cct gaa ggc tct gtt atc tac cct ggt gtt gtg tct cac 336 Asn Lys Leu Pro Glu Gly Ser Val Ile Tyr Pro Gly Val Val Ser His 100 105 110 tcc atc aac gct gtg gag cac cca cgc ctg gtt gct gat cgt atc gtt 384 Ser Ile Asn Ala Val Glu His Pro Arg Leu Val Ala Asp Arg Ile Val 115 120 125 cag ttc gcc aag ctt gtt ggc cct gag aac gtc att gcg tcc act gac 432 Gln Phe Ala Lys Leu Val Gly Pro Glu Asn Val Ile Ala Ser Thr Asp 130 135 140 tgt ggt ctg ggc gga cgt ctg cat tcc cag atc gca tgg gca aag ctg 480 Cys Gly Leu Gly Gly Arg Leu His Ser Gln Ile Ala Trp Ala Lys Leu 145 150 155 160 gag tcc cta gta gag ggc gct cgc att gca tca aag gaa ctg ttc 525 Glu Ser Leu Val Glu Gly Ala Arg Ile Ala Ser Lys Glu Leu Phe 165 170 175 taagctagac aacgagggtt gct 548 112 175 PRT Corynebacterium glutamicum 112 Asp Ala Pro Asp Leu Ala Glu Ala Trp Asp Gln Ile Asn Pro Glu Pro 1 5 10 15 Ser Val Lys Asp Tyr Leu Asp Trp Ile Gly Thr Arg Ile Asp Ala Ile 20 25 30 Asn Ser Ala Val Lys Gly Leu Pro Lys Glu Gln Thr Arg Leu His Ile 35 40 45 Cys Trp Gly Ser Trp His Gly Pro His Val Thr Asp Ile Pro Phe Gly 50 55 60 Asp Ile Ile Gly Glu Ile Leu Arg Ala Glu Val Gly Gly Phe Ser Phe 65 70 75 80 Glu Gly Ala Ser Pro Arg His Ala His Glu Trp Arg Val Trp Glu Glu 85 90 95 Asn Lys Leu Pro Glu Gly Ser Val Ile Tyr Pro Gly Val Val Ser His 100 105 110 Ser Ile Asn Ala Val Glu His Pro Arg Leu Val Ala Asp Arg Ile Val 115 120 125 Gln Phe Ala Lys Leu Val Gly Pro Glu Asn Val Ile Ala Ser Thr Asp 130 135 140 Cys Gly Leu Gly Gly Arg Leu His Ser Gln Ile Ala Trp Ala Lys Leu 145 150 155 160 Glu Ser Leu Val Glu Gly Ala Arg Ile Ala Ser Lys Glu Leu Phe 165 170 175 113 784 DNA Corynebacterium glutamicum CDS (101)..(784) FRXA02658 113 atgaataaaa ttccgggtgc agtgaccgta ggtgaggtaa acgcggttag agtcgaatga 60 gagtttgata ctttctttcg acttttagat tggattttca atg agc cag aac cgc 115 Met Ser Gln Asn Arg 1 5 atc agg acc act cac gtt ggt tcc ttg ccc cgt acc cca gag cta ctt 163 Ile Arg Thr Thr His Val Gly Ser Leu Pro Arg Thr Pro Glu Leu Leu 10 15 20 gat gca aac atc aag cgt tct aac ggt gag att ggg gag gag gaa ttc 211 Asp Ala Asn Ile Lys Arg Ser Asn Gly Glu Ile Gly Glu Glu Glu Phe 25 30 35 ttc cag att ctg cag tct tct gta gat gac gtg atc aag cgc cag gtt 259 Phe Gln Ile Leu Gln Ser Ser Val Asp Asp Val Ile Lys Arg Gln Val 40 45 50 gac ctg ggt atc gac atc ctt aac gag ggc gaa tac ggc cac gtc acc 307 Asp Leu Gly Ile Asp Ile Leu Asn Glu Gly Glu Tyr Gly His Val Thr 55 60 65 tcc ggt gca gtt gac ttc ggt gca tgg tgg aac tac tcc ttc acc cgc 355 Ser Gly Ala Val Asp Phe Gly Ala Trp Trp Asn Tyr Ser Phe Thr Arg 70 75 80 85 ctg ggc gga ctg acc atg acc gat acc gac cgt tgg gca agc cag gaa 403 Leu Gly Gly Leu Thr Met Thr Asp Thr Asp Arg Trp Ala Ser Gln Glu 90 95 100 gca gtg cgt tcc acc cct ggc aac atc gag ctg acc agc ttc tct gat 451 Ala Val Arg Ser Thr Pro Gly Asn Ile Glu Leu Thr Ser Phe Ser Asp 105 110 115 cgt cgc gac cgc gca ttg ttc agc gaa gca tac gag gat cca gta tct 499 Arg Arg Asp Arg Ala Leu Phe Ser Glu Ala Tyr Glu Asp Pro Val Ser 120 125 130 ggc atc ttc acc ggt cgc gct tct gtg ggc aac cca gag ttc acc gga 547 Gly Ile Phe Thr Gly Arg Ala Ser Val Gly Asn Pro Glu Phe Thr Gly 135 140 145 cct att acc tac att ggc cag gaa gaa act cag acg gat gtt gat ctg 595 Pro Ile Thr Tyr Ile Gly Gln Glu Glu Thr Gln Thr Asp Val Asp Leu 150 155 160 165 ctg aag aag ggc atg aac gca gcg gga gct acc gac ggc ttc gtt gca 643 Leu Lys Lys Gly Met Asn Ala Ala Gly Ala Thr Asp Gly Phe Val Ala 170 175 180 gca cta tcc cca gga tct gca gct cga ttg acc aac aag ttc tac gac 691 Ala Leu Ser Pro Gly Ser Ala Ala Arg Leu Thr Asn Lys Phe Tyr Asp 185 190 195 act gat gaa gaa gtc gtc gca gca tgt gct gat gcg ctt tcc cag gaa 739 Thr Asp Glu Glu Val Val Ala Ala Cys Ala Asp Ala Leu Ser Gln Glu 200 205 210 tac aag atc atc acc gat gca ggt ctg acc gtt cag ctc gac gca 784 Tyr Lys Ile Ile Thr Asp Ala Gly Leu Thr Val Gln Leu Asp Ala 215 220 225 114 228 PRT Corynebacterium glutamicum 114 Met Ser Gln Asn Arg Ile Arg Thr Thr His Val Gly Ser Leu Pro Arg 1 5 10 15 Thr Pro Glu Leu Leu Asp Ala Asn Ile Lys Arg Ser Asn Gly Glu Ile 20 25 30 Gly Glu Glu Glu Phe Phe Gln Ile Leu Gln Ser Ser Val Asp Asp Val 35 40 45 Ile Lys Arg Gln Val Asp Leu Gly Ile Asp Ile Leu Asn Glu Gly Glu 50 55 60 Tyr Gly His Val Thr Ser Gly Ala Val Asp Phe Gly Ala Trp Trp Asn 65 70 75 80 Tyr Ser Phe Thr Arg Leu Gly Gly Leu Thr Met Thr Asp Thr Asp Arg 85 90 95 Trp Ala Ser Gln Glu Ala Val Arg Ser Thr Pro Gly Asn Ile Glu Leu 100 105 110 Thr Ser Phe Ser Asp Arg Arg Asp Arg Ala Leu Phe Ser Glu Ala Tyr 115 120 125 Glu Asp Pro Val Ser Gly Ile Phe Thr Gly Arg Ala Ser Val Gly Asn 130 135 140 Pro Glu Phe Thr Gly Pro Ile Thr Tyr Ile Gly Gln Glu Glu Thr Gln 145 150 155 160 Thr Asp Val Asp Leu Leu Lys Lys Gly Met Asn Ala Ala Gly Ala Thr 165 170 175 Asp Gly Phe Val Ala Ala Leu Ser Pro Gly Ser Ala Ala Arg Leu Thr 180 185 190 Asn Lys Phe Tyr Asp Thr Asp Glu Glu Val Val Ala Ala Cys Ala Asp 195 200 205 Ala Leu Ser Gln Glu Tyr Lys Ile Ile Thr Asp Ala Gly Leu Thr Val 210 215 220 Gln Leu Asp Ala 225 115 408 DNA Corynebacterium glutamicum CDS (101)..(385) RXC02238 115 ggcgcttagc caaaacatag agcggtaggg tatgcttatc cgattgagca acctttcccg 60 ctcttaacac tactgtccat atacttttga aaaggtgtca gtg acc aac gtg agc 115 Val Thr Asn Val Ser 1 5 aac gag acc aac gcc acc aag gcc gtc ttc gat ccg cca gtg ggc att 163 Asn Glu Thr Asn Ala Thr Lys Ala Val Phe Asp Pro Pro Val Gly Ile 10 15 20 acc gct cct ccg atc gat gaa ctg ctg gat aag gtc act tcc aag tac 211 Thr Ala Pro Pro Ile Asp Glu Leu Leu Asp Lys Val Thr Ser Lys Tyr 25 30 35 gcc ctc gtg atc ttc gca gcc aag cgt gcg cgc cag atc aac agc ttc 259 Ala Leu Val Ile Phe Ala Ala Lys Arg Ala Arg Gln Ile Asn Ser Phe 40 45 50 tac cat cag gca gat gag gga gta ttc gag ttc atc gga cca ttg gtt 307 Tyr His Gln Ala Asp Glu Gly Val Phe Glu Phe Ile Gly Pro Leu Val 55 60 65 act ccg cag cca ggc gaa aag cca ctt tct att gct ctg cgt gag atc 355 Thr Pro Gln Pro Gly Glu Lys Pro Leu Ser Ile Ala Leu Arg Glu Ile 70 75 80 85 aat gca ggt ctg ttg gac cac gag gaa ggt taaaagacct tataacttca 405 Asn Ala Gly Leu Leu Asp His Glu Glu Gly 90 95 cac 408 116 95 PRT Corynebacterium glutamicum 116 Val Thr Asn Val Ser Asn Glu Thr Asn Ala Thr Lys Ala Val Phe Asp 1 5 10 15 Pro Pro Val Gly Ile Thr Ala Pro Pro Ile Asp Glu Leu Leu Asp Lys 20 25 30 Val Thr Ser Lys Tyr Ala Leu Val Ile Phe Ala Ala Lys Arg Ala Arg 35 40 45 Gln Ile Asn Ser Phe Tyr His Gln Ala Asp Glu Gly Val Phe Glu Phe 50 55 60 Ile Gly Pro Leu Val Thr Pro Gln Pro Gly Glu Lys Pro Leu Ser Ile 65 70 75 80 Ala Leu Arg Glu Ile Asn Ala Gly Leu Leu Asp His Glu Glu Gly 85 90 95 117 1827 DNA Corynebacterium glutamicum CDS (101)..(1804) RXC00128 117 ccattttccg tttggtcttg cctaaagaac cgcatggaaa ttatcgtgaa gcaccgatcc 60 cgttgatcgc tccagagaca ccgtgggaag gggagcagca gtg agt aaa att tcg 115 Val Ser Lys Ile Ser 1 5 acg aaa ctg aag gcc ctc acc gcg gtg ctg tct gtg acc act ctg gtg 163 Thr Lys Leu Lys Ala Leu Thr Ala Val Leu Ser Val Thr Thr Leu Val 10 15 20 gct ggg tgt tcc acg ctt ccg cag aac acg gat ccg caa gtg ctg cgc 211 Ala Gly Cys Ser Thr Leu Pro Gln Asn Thr Asp Pro Gln Val Leu Arg 25 30 35 tca ttt tcc ggg tcc caa agc aca caa gag ata gca ggg ccg acc ccg 259 Ser Phe Ser Gly Ser Gln Ser Thr Gln Glu Ile Ala Gly Pro Thr Pro 40 45 50 aat caa gat ccg gat ttg ttg atc cgc ggc ttc ttc agc gca ggt gcg 307 Asn Gln Asp Pro Asp Leu Leu Ile Arg Gly Phe Phe Ser Ala Gly Ala 55 60 65 tat ccg act cag cag tat gaa gcg gcg aag gcg tat ctg acg gaa ggg 355 Tyr Pro Thr Gln Gln Tyr Glu Ala Ala Lys Ala Tyr Leu Thr Glu Gly 70 75 80 85 acg cgc agc acg tgg aat ccg gct gcg tcg act cgt att ttg gat cgc 403 Thr Arg Ser Thr Trp Asn Pro Ala Ala Ser Thr Arg Ile Leu Asp Arg 90 95 100 att gat ctg aac act ctg cca ggt tcg acg aat gcg gaa cga acg att 451 Ile Asp Leu Asn Thr Leu Pro Gly Ser Thr Asn Ala Glu Arg Thr Ile 105 110 115 gcg atc cgt gga acg cag gtc gga acg ttg ctc agc ggt ggc gtg tat 499 Ala Ile Arg Gly Thr Gln Val Gly Thr Leu Leu Ser Gly Gly Val Tyr 120 125 130 cag ccg gag aat gcg gag ttt gaa gct gag atc acg atg cgt cgg gaa 547 Gln Pro Glu Asn Ala Glu Phe Glu Ala Glu Ile Thr Met Arg Arg Glu 135 140 145 gat ggg gag tgg cgt atc gat gct ttg ccg gac ggg att tta tta gag 595 Asp Gly Glu Trp Arg Ile Asp Ala Leu Pro Asp Gly Ile Leu Leu Glu 150 155 160 165 aga aac gat ctg cgg aac cat tac act ccg cac gat gtg tat ttc ttt 643 Arg Asn Asp Leu Arg Asn His Tyr Thr Pro His Asp Val Tyr Phe Phe 170 175 180 gat cct tct ggc cag gtg ttg gtg ggg gat cgg cgt tgg ttg ttc aat 691 Asp Pro Ser Gly Gln Val Leu Val Gly Asp Arg Arg Trp Leu Phe Asn 185 190 195 gag tcg cag tcg atg tcc acg gtg ctg atg gcc ctt ctg gtt aat ggt 739 Glu Ser Gln Ser Met Ser Thr Val Leu Met Ala Leu Leu Val Asn Gly 200 205 210 cct tcg ccg gca att tct cct ggt gtg gtc aat cag ctg tcc acg gat 787 Pro Ser Pro Ala Ile Ser Pro Gly Val Val Asn Gln Leu Ser Thr Asp 215 220 225 gcg tcg ttc gtg ggg ttc aat gat ggg gag tat cag ttc act ggt ttg 835 Ala Ser Phe Val Gly Phe Asn Asp Gly Glu Tyr Gln Phe Thr Gly Leu 230 235 240 245 gga aat ttg gat gat gat gcg cgt ttg cgt ttc gcc gcc cag gcc gtg 883 Gly Asn Leu Asp Asp Asp Ala Arg Leu Arg Phe Ala Ala Gln Ala Val 250 255 260 tgg acg ttg gcg cat gct gat gtc gca ggc ccc tac act ttg gtc gct 931 Trp Thr Leu Ala His Ala Asp Val Ala Gly Pro Tyr Thr Leu Val Ala 265 270 275 gac ggc gcg ccg ttg ctg tcg gag ttc cca acg ctc acc acc gat gac 979 Asp Gly Ala Pro Leu Leu Ser Glu Phe Pro Thr Leu Thr Thr Asp Asp 280 285 290 ctc gcc gaa tac aac cca gag gct tac acc aac acg gtg tcc acg ttg 1027 Leu Ala Glu Tyr Asn Pro Glu Ala Tyr Thr Asn Thr Val Ser Thr Leu 295 300 305 ttt gcg ttg cag gat gga tcg ttg tcg agg gtc agt tcc ggc aat gtg 1075 Phe Ala Leu Gln Asp Gly Ser Leu Ser Arg Val Ser Ser Gly Asn Val 310 315 320 325 agt cca cta cag ggc att tgg agc ggt gga gat atc gat tct gca gcg 1123 Ser Pro Leu Gln Gly Ile Trp Ser Gly Gly Asp Ile Asp Ser Ala Ala 330 335 340 att tcc tcc tcc gcc aat gtg gtg gca gcg gta cgc cac gaa aac aac 1171 Ile Ser Ser Ser Ala Asn Val Val Ala Ala Val Arg His Glu Asn Asn 345 350 355 gag gca gtg ctt act gtt ggc tcc atg gaa ggc gtg act tca gat gcg 1219 Glu Ala Val Leu Thr Val Gly Ser Met Glu Gly Val Thr Ser Asp Ala 360 365 370 ttg agg agt gaa acg atc act cgt ccc acc ttt gaa tac gcg tcg agt 1267 Leu Arg Ser Glu Thr Ile Thr Arg Pro Thr Phe Glu Tyr Ala Ser Ser 375 380 385 ggg ttg tgg gct gtg gtg gat ggg gag acg cct gtc cga gtc gca cga 1315 Gly Leu Trp Ala Val Val Asp Gly Glu Thr Pro Val Arg Val Ala Arg 390 395 400 405 tcg gca aca acc ggt gag ctc gtc cag acg gag gcg gag att gtg ctg 1363 Ser Ala Thr Thr Gly Glu Leu Val Gln Thr Glu Ala Glu Ile Val Leu 410 415 420 cca agg gat gtg acg ggt ccg atc tct gaa ttc caa ctg tca cga act 1411 Pro Arg Asp Val Thr Gly Pro Ile Ser Glu Phe Gln Leu Ser Arg Thr 425 430 435 ggg gtc cgg gcc gcc atg atc att gaa ggc aag gtg tac gtg ggc gtc 1459 Gly Val Arg Ala Ala Met Ile Ile Glu Gly Lys Val Tyr Val Gly Val 440 445 450 gta acg cgt cct ggt ccg ggc gag cgg cgc gtg aca aat atc acg gag 1507 Val Thr Arg Pro Gly Pro Gly Glu Arg Arg Val Thr Asn Ile Thr Glu 455 460 465 gtg gcg ccg agc ttg ggc gag gcg gcg ctg tcg atc aac tgg cgc cca 1555 Val Ala Pro Ser Leu Gly Glu Ala Ala Leu Ser Ile Asn Trp Arg Pro 470 475 480 485 gac ggc att ttg ctt gtg ggc acg tca att cca gag acg ccg ctg tgg 1603 Asp Gly Ile Leu Leu Val Gly Thr Ser Ile Pro Glu Thr Pro Leu Trp 490 495 500 cgc gtc gag cag gac gga tcg gcg att tcg tcg atg ccg agc ggg aat 1651 Arg Val Glu Gln Asp Gly Ser Ala Ile Ser Ser Met Pro Ser Gly Asn 505 510 515 ctc agc gcg ccg gtg gtg gcg gtg gca agt tcc gcg acg acg gtc tac 1699 Leu Ser Ala Pro Val Val Ala Val Ala Ser Ser Ala Thr Thr Val Tyr 520 525 530 gtc act gat tcg cat gcg atg ctt cag ctg ccg act gcc gat aat gat 1747 Val Thr Asp Ser His Ala Met Leu Gln Leu Pro Thr Ala Asp Asn Asp 535 540 545 att tgg cgc gag gtg ccc ggt ttg ctg ggc acg cgt gcg gcg ccg gtg 1795 Ile Trp Arg Glu Val Pro Gly Leu Leu Gly Thr Arg Ala Ala Pro Val 550 555 560 565 gtt gcg tac tgatggagct gttcttcccg cgc 1827 Val Ala Tyr 118 568 PRT Corynebacterium glutamicum 118 Val Ser Lys Ile Ser Thr Lys Leu Lys Ala Leu Thr Ala Val Leu Ser 1 5 10 15 Val Thr Thr Leu Val Ala Gly Cys Ser Thr Leu Pro Gln Asn Thr Asp 20 25 30 Pro Gln Val Leu Arg Ser Phe Ser Gly Ser Gln Ser Thr Gln Glu Ile 35 40 45 Ala Gly Pro Thr Pro Asn Gln Asp Pro Asp Leu Leu Ile Arg Gly Phe 50 55 60 Phe Ser Ala Gly Ala Tyr Pro Thr Gln Gln Tyr Glu Ala Ala Lys Ala 65 70 75 80 Tyr Leu Thr Glu Gly Thr Arg Ser Thr Trp Asn Pro Ala Ala Ser Thr 85 90 95 Arg Ile Leu Asp Arg Ile Asp Leu Asn Thr Leu Pro Gly Ser Thr Asn 100 105 110 Ala Glu Arg Thr Ile Ala Ile Arg Gly Thr Gln Val Gly Thr Leu Leu 115 120 125 Ser Gly Gly Val Tyr Gln Pro Glu Asn Ala Glu Phe Glu Ala Glu Ile 130 135 140 Thr Met Arg Arg Glu Asp Gly Glu Trp Arg Ile Asp Ala Leu Pro Asp 145 150 155 160 Gly Ile Leu Leu Glu Arg Asn Asp Leu Arg Asn His Tyr Thr Pro His 165 170 175 Asp Val Tyr Phe Phe Asp Pro Ser Gly Gln Val Leu Val Gly Asp Arg 180 185 190 Arg Trp Leu Phe Asn Glu Ser Gln Ser Met Ser Thr Val Leu Met Ala 195 200 205 Leu Leu Val Asn Gly Pro Ser Pro Ala Ile Ser Pro Gly Val Val Asn 210 215 220 Gln Leu Ser Thr Asp Ala Ser Phe Val Gly Phe Asn Asp Gly Glu Tyr 225 230 235 240 Gln Phe Thr Gly Leu Gly Asn Leu Asp Asp Asp Ala Arg Leu Arg Phe 245 250 255 Ala Ala Gln Ala Val Trp Thr Leu Ala His Ala Asp Val Ala Gly Pro 260 265 270 Tyr Thr Leu Val Ala Asp Gly Ala Pro Leu Leu Ser Glu Phe Pro Thr 275 280 285 Leu Thr Thr Asp Asp Leu Ala Glu Tyr Asn Pro Glu Ala Tyr Thr Asn 290 295 300 Thr Val Ser Thr Leu Phe Ala Leu Gln Asp Gly Ser Leu Ser Arg Val 305 310 315 320 Ser Ser Gly Asn Val Ser Pro Leu Gln Gly Ile Trp Ser Gly Gly Asp 325 330 335 Ile Asp Ser Ala Ala Ile Ser Ser Ser Ala Asn Val Val Ala Ala Val 340 345 350 Arg His Glu Asn Asn Glu Ala Val Leu Thr Val Gly Ser Met Glu Gly 355 360 365 Val Thr Ser Asp Ala Leu Arg Ser Glu Thr Ile Thr Arg Pro Thr Phe 370 375 380 Glu Tyr Ala Ser Ser Gly Leu Trp Ala Val Val Asp Gly Glu Thr Pro 385 390 395 400 Val Arg Val Ala Arg Ser Ala Thr Thr Gly Glu Leu Val Gln Thr Glu 405 410 415 Ala Glu Ile Val Leu Pro Arg Asp Val Thr Gly Pro Ile Ser Glu Phe 420 425 430 Gln Leu Ser Arg Thr Gly Val Arg Ala Ala Met Ile Ile Glu Gly Lys 435 440 445 Val Tyr Val Gly Val Val Thr Arg Pro Gly Pro Gly Glu Arg Arg Val 450 455 460 Thr Asn Ile Thr Glu Val Ala Pro Ser Leu Gly Glu Ala Ala Leu Ser 465 470 475 480 Ile Asn Trp Arg Pro Asp Gly Ile Leu Leu Val Gly Thr Ser Ile Pro 485 490 495 Glu Thr Pro Leu Trp Arg Val Glu Gln Asp Gly Ser Ala Ile Ser Ser 500 505 510 Met Pro Ser Gly Asn Leu Ser Ala Pro Val Val Ala Val Ala Ser Ser 515 520 525 Ala Thr Thr Val Tyr Val Thr Asp Ser His Ala Met Leu Gln Leu Pro 530 535 540 Thr Ala Asp Asn Asp Ile Trp Arg Glu Val Pro Gly Leu Leu Gly Thr 545 550 555 560 Arg Ala Ala Pro Val Val Ala Tyr 565 119 1344 DNA Corynebacterium glutamicum CDS (101)..(1321) RXA02240 119 cagctagacc actgacattg cagttttaga cagcttggtc tatattggtt ttttgtattt 60 aagactattt attctcaact tcttcgaaag aagggtattt gtg gct cag cca acc 115 Val Ala Gln Pro Thr 1 5 gcc gtc cgt ttg ttc acc agt gaa tct gta act gag gga cat cca gac 163 Ala Val Arg Leu Phe Thr Ser Glu Ser Val Thr Glu Gly His Pro Asp 10 15 20 aaa ata tgt gat gct att tcc gat acc att ttg gac gcg ctg ctc gaa 211 Lys Ile Cys Asp Ala Ile Ser Asp Thr Ile Leu Asp Ala Leu Leu Glu 25 30 35 aaa gat ccg cag tcg cgc gtc gca gtg gaa act gtg gtc acc acc gga 259 Lys Asp Pro Gln Ser Arg Val Ala Val Glu Thr Val Val Thr Thr Gly 40 45 50 atc gtc cat gtt gtt ggc gag gtc cgt acc agc gct tac gta gag atc 307 Ile Val His Val Val Gly Glu Val Arg Thr Ser Ala Tyr Val Glu Ile 55 60 65 cct caa tta gtc cgc aac aag ctc atc gaa atc gga ttc aac tcc tct 355 Pro Gln Leu Val Arg Asn Lys Leu Ile Glu Ile Gly Phe Asn Ser Ser 70 75 80 85 gag gtt gga ttc gac gga cgc acc tgt ggc gtc tca gta tcc atc ggt 403 Glu Val Gly Phe Asp Gly Arg Thr Cys Gly Val Ser Val Ser Ile Gly 90 95 100 gag cag tcc cag gaa atc gct gac ggc gtg gat aac tcc gac gaa gcc 451 Glu Gln Ser Gln Glu Ile Ala Asp Gly Val Asp Asn Ser Asp Glu Ala 105 110 115 cgc acc aac ggc gac gtt gaa gaa gac gac cgc gca ggt gct ggc gac 499 Arg Thr Asn Gly Asp Val Glu Glu Asp Asp Arg Ala Gly Ala Gly Asp 120 125 130 cag ggc ctg atg ttc ggc tac gcc acc aac gaa acc gaa gag tac atg 547 Gln Gly Leu Met Phe Gly Tyr Ala Thr Asn Glu Thr Glu Glu Tyr Met 135 140 145 cct ctt cct atc gcg ttg gcg cac cga ctg tca cgt cgt ctg acc cag 595 Pro Leu Pro Ile Ala Leu Ala His Arg Leu Ser Arg Arg Leu Thr Gln 150 155 160 165 gtt cgt aaa gag ggc atc gtt cct cac ctg cgt cca gac gga aaa acc 643 Val Arg Lys Glu Gly Ile Val Pro His Leu Arg Pro Asp Gly Lys Thr 170 175 180 cag gtc acc ttc gca tac gat gcg caa gac cgc cct agc cac ctg gat 691 Gln Val Thr Phe Ala Tyr Asp Ala Gln Asp Arg Pro Ser His Leu Asp 185 190 195 acc gtt gtc atc tcc acc cag cac gac cca gaa gtt gac cgt gca tgg 739 Thr Val Val Ile Ser Thr Gln His Asp Pro Glu Val Asp Arg Ala Trp 200 205 210 ttg gaa acc caa ctg cgc gaa cac gtc att gat tgg gta atc aaa gac 787 Leu Glu Thr Gln Leu Arg Glu His Val Ile Asp Trp Val Ile Lys Asp 215 220 225 gca ggc att gag gat ctg gca acc ggt gag atc acc gtg ttg atc aac 835 Ala Gly Ile Glu Asp Leu Ala Thr Gly Glu Ile Thr Val Leu Ile Asn 230 235 240 245 cct tca ggt tcc ttc att ctg ggt ggc ccc atg ggt gat gcg ggt ctg 883 Pro Ser Gly Ser Phe Ile Leu Gly Gly Pro Met Gly Asp Ala Gly Leu 250 255 260 acc ggc cgc aag atc atc gtg gat acc tac ggt ggc atg gct cgc cat 931 Thr Gly Arg Lys Ile Ile Val Asp Thr Tyr Gly Gly Met Ala Arg His 265 270 275 ggt ggt gga gca ttc tcc ggt aag gat cca agc aag gtg gac cgc tct 979 Gly Gly Gly Ala Phe Ser Gly Lys Asp Pro Ser Lys Val Asp Arg Ser 280 285 290 gct gca tac gcc atg cgt tgg gta gca aag aac atc gtg gca gca ggc 1027 Ala Ala Tyr Ala Met Arg Trp Val Ala Lys Asn Ile Val Ala Ala Gly 295 300 305 ctt gct gat cgc gct gaa gtt cag gtt gca tac gcc att gga cgc gca 1075 Leu Ala Asp Arg Ala Glu Val Gln Val Ala Tyr Ala Ile Gly Arg Ala 310 315 320 325 aag cca gtc gga ctt tac gtt gaa acc ttt gac acc aac aag gaa ggc 1123 Lys Pro Val Gly Leu Tyr Val Glu Thr Phe Asp Thr Asn Lys Glu Gly 330 335 340 ctg agc gac gag cag att cag gct gcc gtg ttg gag gtc ttt gac ctg 1171 Leu Ser Asp Glu Gln Ile Gln Ala Ala Val Leu Glu Val Phe Asp Leu 345 350 355 cgt cca gca gca att atc cgt gag ctt gat ctg ctt cgt ccg atc tac 1219 Arg Pro Ala Ala Ile Ile Arg Glu Leu Asp Leu Leu Arg Pro Ile Tyr 360 365 370 gct gac act gct gcc tac ggc cac ttt ggt cgc act gat ttg gac ctt 1267 Ala Asp Thr Ala Ala Tyr Gly His Phe Gly Arg Thr Asp Leu Asp Leu 375 380 385 cct tgg gag gct atc gac cgc gtt gat gaa ctt cgc gca gcc ctc aag 1315 Pro Trp Glu Ala Ile Asp Arg Val Asp Glu Leu Arg Ala Ala Leu Lys 390 395 400 405 ttg gcc taaaaatctg atgtagtatc ttc 1344 Leu Ala 120 407 PRT Corynebacterium glutamicum 120 Val Ala Gln Pro Thr Ala Val Arg Leu Phe Thr Ser Glu Ser Val Thr 1 5 10 15 Glu Gly His Pro Asp Lys Ile Cys Asp Ala Ile Ser Asp Thr Ile Leu 20 25 30 Asp Ala Leu Leu Glu Lys Asp Pro Gln Ser Arg Val Ala Val Glu Thr 35 40 45 Val Val Thr Thr Gly Ile Val His Val Val Gly Glu Val Arg Thr Ser 50 55 60 Ala Tyr Val Glu Ile Pro Gln Leu Val Arg Asn Lys Leu Ile Glu Ile 65 70 75 80 Gly Phe Asn Ser Ser Glu Val Gly Phe Asp Gly Arg Thr Cys Gly Val 85 90 95 Ser Val Ser Ile Gly Glu Gln Ser Gln Glu Ile Ala Asp Gly Val Asp 100 105 110 Asn Ser Asp Glu Ala Arg Thr Asn Gly Asp Val Glu Glu Asp Asp Arg 115 120 125 Ala Gly Ala Gly Asp Gln Gly Leu Met Phe Gly Tyr Ala Thr Asn Glu 130 135 140 Thr Glu Glu Tyr Met Pro Leu Pro Ile Ala Leu Ala His Arg Leu Ser 145 150 155 160 Arg Arg Leu Thr Gln Val Arg Lys Glu Gly Ile Val Pro His Leu Arg 165 170 175 Pro Asp Gly Lys Thr Gln Val Thr Phe Ala Tyr Asp Ala Gln Asp Arg 180 185 190 Pro Ser His Leu Asp Thr Val Val Ile Ser Thr Gln His Asp Pro Glu 195 200 205 Val Asp Arg Ala Trp Leu Glu Thr Gln Leu Arg Glu His Val Ile Asp 210 215 220 Trp Val Ile Lys Asp Ala Gly Ile Glu Asp Leu Ala Thr Gly Glu Ile 225 230 235 240 Thr Val Leu Ile Asn Pro Ser Gly Ser Phe Ile Leu Gly Gly Pro Met 245 250 255 Gly Asp Ala Gly Leu Thr Gly Arg Lys Ile Ile Val Asp Thr Tyr Gly 260 265 270 Gly Met Ala Arg His Gly Gly Gly Ala Phe Ser Gly Lys Asp Pro Ser 275 280 285 Lys Val Asp Arg Ser Ala Ala Tyr Ala Met Arg Trp Val Ala Lys Asn 290 295 300 Ile Val Ala Ala Gly Leu Ala Asp Arg Ala Glu Val Gln Val Ala Tyr 305 310 315 320 Ala Ile Gly Arg Ala Lys Pro Val Gly Leu Tyr Val Glu Thr Phe Asp 325 330 335 Thr Asn Lys Glu Gly Leu Ser Asp Glu Gln Ile Gln Ala Ala Val Leu 340 345 350 Glu Val Phe Asp Leu Arg Pro Ala Ala Ile Ile Arg Glu Leu Asp Leu 355 360 365 Leu Arg Pro Ile Tyr Ala Asp Thr Ala Ala Tyr Gly His Phe Gly Arg 370 375 380 Thr Asp Leu Asp Leu Pro Trp Glu Ala Ile Asp Arg Val Asp Glu Leu 385 390 395 400 Arg Ala Ala Leu Lys Leu Ala 405 121 24 DNA Artificial Sequence Description of Artificial Sequence primer 121 tcgggtatcc gcgctacact taga 24 122 23 DNA Artificial Sequence Description of Artificial Sequence primer 122 ggaaaccggg gcatcgaaac tta 23 123 18 DNA Artificial Sequence Description of Artificial Sequence primer 123 ggaaacagta tgaccatg 18 124 17 DNA Artificial Sequence Description of Artificial Sequence primer 124 gtaaaacgac ggccagt 17 125 4334 DNA Corynebacterium glutamicum 125 aaatcgcttg accattgcag gttggtttat gactgttgag ggagagactg gctcgtggcc 60 gacaatcaat gaagctatgt ctgaatttag cgtgtcacgt cagaccgtga atagagcact 120 taagtctgcg ggcattgaac ttccacgagg acgccgtaaa gcttcccagt aaatgtgcca 180 tctcgtaggc agaaaacggt tccccccgta ggggtctctc tcttggcctc ctttctaggt 240 cgggctgatt gctcttgaag ctctctaggg gggctcacac cataggcaga taacggttcc 300 ccaccggctc acctcgtaag cgcacaagga ctgctcccaa agatcttcaa agccactgcc 360 gcgactccgc ttcgcgaagc cttgccccgc ggaaatttcc tccaccgagt tcgtgcacac 420 ccctatgcca agcttctttc accctaaatt cgagagattg gattcttacc gtggaaattc 480 ttcgcaaaaa tcgtcccctg atcgcccttg cgacgttgct cgcggcggtg ccgctggttg 540 cgcttggctt gaccgacttg atcagcttgc atgcctgcag gtcgacggat ccccgggtgg 600 gaaagccacg ttgtgtctca aaatctctga tgttacattg cacaagataa aaatatatca 660 tcatgaacaa taaaactgtc tgcttacata aacagtaata caaggggtgt tatgagccat 720 attcaacggg aaacgtcttg ctcgaggccg cgattaaatt ccaacatgga tgctgattta 780 tatgggtata aatgggctcg cgataatgtc gggcaatcag gtgcgacaat ctatcgattg 840 tatgggaagc ccgatgcgcc agagttgttt ctgaaacatg gcaaaggtag cgttgccaat 900 gatgttacag atgagatggt cagactaaac tggctgacgg aatttatgcc tcttccgacc 960 atcaagcatt ttatccgtac tcctgatgat gcatggttac tcaccactgc gatccccggg 1020 aaaacagcat tccaggtatt agaagaatat cctgattcag gtgaaaatat tgttgatgcg 1080 ctggcagtgt tcctgcgccg gttgcattcg attcctgttt gtaattgtcc ttttaacagc 1140 gatcgcgtat ttcgtctcgc tcaggcgcaa tcacgaatga ataacggttt ggttgatgcg 1200 agtgattttg atgacgagcg taatggctgg cctgttgaac aagtctggaa agaaatgcat 1260 aagcttttgc cattctcacc ggattcagtc gtcactcatg gtgatttctc acttgataac 1320 cttatttttg acgaggggaa attaataggt tgtattgatg ttggacgagt cggaatcgca 1380 gaccgatacc aggatcttgc catcctatgg aactgcctcg gtgagttttc tccttcatta 1440 cagaaacggc tttttcaaaa atatggtatt gataatcctg atatgaataa attgcagttt 1500 catttgatgc tcgatgagtt tttctaatca gaattggtta attggttgta acactggcag 1560 agcattacgc tgacttgacg ggacggcggc tttgttgaat aaatcgaact tttgctgagt 1620 tgaaggatca gatcacgcat cttcccgaca acgcagaccg ttccgtggca aagcaaaagt 1680 tcaaaatcac caactggtcc acctacaaca aagctctcat caaccgtggc tccctcactt 1740 tctggctgga tgatggggcg attcaggcct ggtatgagtc agcaacacct tcttcacgag 1800 gcagacctca gcgcccccga attgatcagt actgcggcgt cgctgatcgc cctcgcgacg 1860 ttgtgcgggt ggcttgtccc tgagggcgct gcgacagata gctaaaaatc tgcgtcagga 1920 tcgccgtaga gcgcgcgtcg cgtcgattgg aggcttcccc tttggttgac ggtcttcaat 1980 cgctctacgg cgatcctgac gcttttttgt tgcgtaccgt cgatcgtttt atttctgtcg 2040 atcccgaaaa agtttttgcc ttttgtaaaa aacttctcgg tcgccccgca aattttcgat 2100 tccagatttt ttaaaaacca agccagaaat acgacacacc gtttgcagat aatctgtctt 2160 tcggaaaaat caagtgcgat acaaaatttt tagcacccct gagctgcgca aagtcccgct 2220 tcgtgaaaat tttcgtgccg cgtgattttc cgccaaaaac tttaacgaac gttcgttata 2280 atggtgtcat gaccttcacg acgaagtacc aaaattggcc cgaatcatca gctatggatc 2340 tctctgatgt cgcgctggag tccgacgcgc tcgatgctgc cgtcgattta aaaacggtga 2400 tcggattttt ccgagctctc gatacgacgg acgcgccagc atcacgagac tgggccagtg 2460 ccgcgagcga cctagaaact ctcgtggcgg atcttgagga gctggctgac gagctgcgtg 2520 ctcggcagcg ccaggaggac gcacagtagt ggaggatcga atcagttgcg cctactgcgg 2580 tggcctgatt cctccccggc ctgacccgcg aggacggcgc gcaaaatatt gctcagatgc 2640 gtgtcgtgcc gcagccagcc gcgagcgcgc caacaaacgc cacgccgagg agctggaggc 2700 ggctaggtcg caaatggcgc tggaagtgcg tcccccgagc gaaattttgg ccatggtcgt 2760 cacagagctg gaagcggcag cgagaattat ccgcgatcgt ggcgcggtgc ccgcaggcat 2820 gacaaacatc gtaaatgccg cgtttcgtgt ggccgtggcc gcccaggacg tgtcagcgcc 2880 gccaccacct gcaccgaatc ggcagcagcg tcgcgcgtcg aaaaagcgca caggcggcaa 2940 gaagcgataa gctgcacgaa tacctgaaaa atgttgaacg ccccgtgagc ggtaactcac 3000 agggcgtcgg ctaaccccca gtccaaacca gggagaaagc gctcaaaaat gactctagcg 3060 gattcacgag acattgacac accggcctgg aaattttccg ctgatctgtt cgacacccat 3120 cccgagctcg cgctgcgatc acgtggctgg acgagcgaag accgccgcga attcctcgct 3180 cacctgggca gagaaaattt ccagggcagc aagacccgcg acttcgccag cgcttggatc 3240 aaagacccgg acacgggaga aacacagccg aagttatacc gagttggttc aaaatcgctt 3300 gcccggtgcc agtatgttgc tctgacgcac gcgcagcacg cagccgtgct tgtcctggac 3360 attgatgtgc cgagccacca ggccggcggg aaaatcgagc acgtaaaccc cgaggtctac 3420 gcgattttgg agcgctgggc acgcctggaa aaagcgccag cttggatcgg cgtgaatcca 3480 ctgagcggga aatgccagct catctggctc attgatccgg tgtatgccgc agcaggcatg 3540 agcagcccga atatgcgcct gctggctgca acgaccgagg aaatgacccg cgttttcggc 3600 gctgaccagg ctttttcaca taggctgagc cggtggccac tgcacgtctc cgacgatccc 3660 accgcgtacc gctggcatgc ccagcacaat cgcgtggatc gcctagctga tcttatggag 3720 gttgctcgca tgatctcagg cacagaaaaa cctaaaaaac gctatgagca ggagttttct 3780 agcggacggg cacgtatcga agcggcaaga aaagccactg cggaagcaaa agcacttgcc 3840 acgcttgaag caagcctgcc gagcgccgct gaagcgtctg gagagctgat cgacggcgtc 3900 cgtgtcctct ggactgctcc agggcgtgcc gcccgtgatg agacggcttt tcgccacgct 3960 ttgactgtgg gataccagtt aaaagcggct ggtgagcgcc taaaagacac caagatcatc 4020 gacgcctacg agcgtgccta caccgtcgct caggcggtcg gagcagacgg ccgtgagcct 4080 gatctgccgc cgatgcgtga ccgccagacg atggcgcgac gtgtgcgcgg ctacgtcgct 4140 aaaggccagc cagtcgtccc tgctcgtcag acagagacgc agagcagccg agggcgaaaa 4200 gctctggcca ctatgggaag acgtggcggt aaaaaggccg cagaacgctg gaaagaccca 4260 aacagtgagt acgcccgagc acagcgagaa aaactagcta agtccagtca acgacaagct 4320 aggaaagcta aagg 4334 

What is claimed:
 1. An isolated nucleic acid molecule from Corynebacterium glutamicum encoding a metabolic pathway protein selected from the group consisting of a nucleic acid molecule comprising the nucleotide sequence set forth in SEQ ID NO: 1, SEQ ID NO:3, or SEQ ID NO:5.
 2. The isolated nucleic acid molecule of claim 1, wherein said metabolic pathway protein is involved in the metabolism of an amino acid.
 3. An isolated nucleic acid molecule which encodes a naturally occurring allelic variant of a polypeptide selected from the group of amino acid sequences consisting of those sequences set forth in SEQ ID NO:2, SEQ ID NO:4, or SEQ ID NO:6.
 4. An isolated nucleic acid molecule comprising a nucleotide sequence which is at least 50% homologous to a nucleotide sequence set forth in SEQ ID NO:6, or a complement thereof.
 5. An isolated nucleic acid molecule comprising a nucleotide sequence which is at least 65% homologous to a nucleotide sequence set forth in SEQ ID NO:1, or a complement thereof.
 6. An isolated nucleic acid molecule comprising a fragment of at least 15 nucleotides of a nucleic acid comprising a nucleotide sequence selected from the group consisting of those sequences set forth set forth in SEQ ID NO: 1, SEQ ID NO:3, or SEQ ID NO:5.
 7. An isolated nucleic acid molecule which hybridizes to the nucleic acid molecule of any one of claims 1-6 under stringent conditions.
 8. An isolated nucleic acid molecule comprising the nucleic acid molecule of claim 1, or a portion thereof, and a nucleotide sequence encoding a heterologous polypeptide.
 9. A vector comprising the nucleic acid molecule of claim
 1. 10. The vector of claim 9, further comprising one or more metabolic pathway nucleic acid molecules.
 11. The vector of claim 9 or 10, which is an expression vector.
 12. A host cell transfected with the expression vector of claim 9 or
 10. 13. The vector of claim 10, wherein the second metabolic pathway nucleic acid molecule is selected from the group consisting of a nucleic acid molecule comprising the nucleotide sequence set forth in the odd-numbered sequences listed in Table 1, excluding any F-designated nucleic acid molecules.
 14. The host cell of claim 12, wherein said cell is a microorganism.
 15. The host cell of claim 12, wherein said cell belongs to the genus Corynebacterium or Brevibacterium.
 16. The host cell of claim 12, wherein the expression of said nucleic acid molecules results in the modulation in production of a fine chemical from said cell.
 17. The host cell of claim 16, wherein said fine chemical is an amino acid.
 18. The host cell of claim 17, wherein said amino acid is methionine or lysine.
 19. A method of producing a polypeptide comprising culturing the host cell of claim 12 in an appropriate culture medium to, thereby, produce the polypeptide.
 20. An isolated metabolic pathway polypeptide from Corynebacterium glutamicum, or a portion thereof.
 21. The protein of claim 20, wherein said polypeptide is selected from the group of metabolic pathway proteins which participate in the metabolism of an amino acid.
 22. The protein of claim 21, wherein said amino acid is methionine or lysine.
 23. An isolated nucleic acid molecule from Corynebacterium glutamicum which encodes a metabolic pathway protein comprising the amino acid sequence set forth in SEQ ID NO:2, SEQ ID NO:4, or SEQ ID NO:6.
 24. An isolated polypeptide comprising a naturally occurring allelic variant of a polypeptide comprising an amino acid sequence selected from the group consisting of those sequences set forth in SEQ ID NO:2, SEQ ID NO:4, or SEQ ID NO:6.
 25. The isolated polypeptide of claim 23, further comprising heterologous amino acid sequences.
 26. An isolated polypeptide comprising a nucleotide sequence which is at least 50% homologous to a nucleotide sequence set forth in SEQ ID NO:5, or a complement thereof.
 27. An isolated polypeptide comprising a nucleotide sequence which is at least 65% homologous to a nucleotide sequence set forth in SEQ ID NO:1, or a complement thereof.
 28. A method for producing a fine chemical, comprising culturing a cell containing a vector of claim 9 or 10, such that the fine chemical is produced.
 29. The method of claim 28, wherein said cell is cultured in the presence of a sulfur source.
 30. The method of claim 28, wherein said method further comprises the step of recovering the fine chemical from said culture.
 31. The method of claim 28, wherein said fine chemical is an amino acid.
 32. The method of claim 31, wherein said amino acid is methionine or lysine.
 33. The method of claim 28, wherein said method further comprises the step of transfecting said cell with the vector of claim 9 or 10, to result in a cell containing said vector.
 34. The method of claim 28, wherein said cell belongs to the genus Corynebacterium or Brevibacterium.
 35. The method of claim 27, wherein said cell is selected from the group consisting of: Corynebacterium glutamicum, Corynebacterium herculis, Corynebacterium, lilium, Corynebacterium acetoacidophilum, Corynebacterium acetoglutamicum, Corynebacterium acetophilum, Corynebacterium ammoniagenes, Corynebacterium fujiokense, Corynebacterium nitrilophilus, Brevibacterium ammoniagenes, Brevibacterium butanicum, Brevibacterium divaricatum, Brevibacterium flavum, Brevibacterium healii, Brevibacterium ketoglutamicum, Brevibacterium ketosoreductum, Brevibacterium lactofermentum, Brevibacterium linens, Brevibacterium paraffinolyticum, and those strains set forth in Table
 3. 36. A method for producing a fine chemical, comprising culturing a cell whose genomic DNA has been altered by the inclusion of a nucleic acid molecule of any one of claims 1-6.
 37. A method for producing a fine chemical, comprising culturing a cell whose genomic DNA has been altered by the inclusion of a nucleic acid molecule of any one of claims 1-6, alone or in combination with another metabolic pathway nucleic acid selected from the group consisting of a nucleic acid molecule comprising the nucleotide sequence set forth in the odd-numbered sequences listed in Table 1, excluding any F-designated nucleic acid molecules.
 38. A method for producing a fine chemical, comprising culturing a cell whose genomic DNA has been altered by the inclusion of a nucleic acid molecule of any one of claims 1-6, alone or in combination with one or more metabolic pathway nucleic acid molecule.
 39. The method of claim 36, wherein the metabolic pathway nucleic acid molecule is selected from the group consisting of metZ, metC, metB, metA, metE, metH, hom, asd, lysC, lysC/ask, rxa00657, dapA, dapB, dapC, dapD/argD, dapE, dapF, lysA, ddh, lysE, lysG, lysR, hsk, ppc, pycA, accD, accA, accB, accC, gpdh genes encoding glucose-6-phophate-dehydrogenase, opcA, pgdh, ta, tk, pgl, rlpe, rpe or any combination of the above-mentioned genes.
 40. The method of claim 35 or 36, wherein said metabolic pathway is methionine or lysine metabolism.
 41. A method of modulating the yield of a fine chemical from a cell comprising, introducing one or more metabolic pathway genes into a cell, thereby modulating the yield of a fine chemical.
 42. The method of claim 41, wherein said metabolic pathway gene or genes are integrated into the chromosome of the cell.
 43. The method of claim 41, wherein said metabolic pathway gene or genes are maintained on a plasmid.
 44. The method of claim 41, wherein said fine chemical is an amino acid.
 45. The method of claim 44, wherein said amino acid is methionine or lysine.
 46. The method of claim 41, wherein said metabolic pathway gene or genes are selected from the group consisting of the nucleic acid molecule of any one of claims 1-6.
 47. The method of claim 41, wherein the nucleotide sequence of said metabolic pathway gene or genes has been mutated to increase yield of a fine chemical. 